The crystallochemistry of tetracyanocomplexes. The crystal and molecular structures of tris(1,2-diaminoethane)zinc(II) tetracyanoniccolate(II) monohydrate and tris(1,2-diaminoethane)zinc(II) tetracyanoniccolate(II)

C₁₀H₂₆N₁₀ONiZn, tris(1,2-diaminoethane) zinc(II) tetrakis(cyano)niccolate(II) monohydrate (I), orthorhombic, Pbca, a = 1.1680(4), b = 1.5844(3), c = 1.9981(6) nm, Z = 8 d(meas) = 1.54, d(calc) = 1.53 g cm^?3. C₁₀H₂₄N₁₀NiZn, tris(1,2-diaminoethane) zinc(II) terakis(cyano)niccolate(II), (II), monoclinic, P2₁/n, a = 0.7957(2), b = 1.5170(5), c = 1.4932(4) nm, β = 96.41(2)°, Z = 4, d(meas) = 1.49, d(calc) = 1.51 g cm^?3. Both the structures (I) and (II) have been solved by the heavy atom method and refined by full-matrix least-squares to R(I) = 0.086 for 1890 independent reflections and R(II) = 0.058 for 1689 independent reflections, respectively. In the case of (II) the superlattice structure problem was solved. The crystal structure of (I) consists of [Zn(en)₃]²⁺ cations, [Ni(CN)₄]^2? anions and water molecules. Two of the cyano groups in trans positions are bonded to water molecules by hydrogen bonds, the distances CN?O being 0.289 and 0.291 nm, respectively. The crystal structure of (II) is constituted by [Zn(en)₃]²⁺ cations and [Ni(CN)₄]^2? anions.     

Identification and characterisation of two distinct acid phosphatases in cell walls of roots of white clover

White clover (Trifolium repens L.) plants were grown in liquid media and subjected to phosphate starvation by removal of the sole phosphate source. After 21 d, roots were harvested and ionically-bound (1 M salt-extractable) cell wall proteins isolated. Two distinct acid phosphatases (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2), designated APase I and II, were identified using hydrophobic column chromatography with each protein consisting of two isoforms resolved by ion-exchange column chromatography. For APase I, both isoforms (IA and IB) are glycosylated (as determined by binding to a monoclonal antibody, mAb 2.23, which is specific to xylose/fucose-containing complex-type N-linked glycans, and a Galanthus nivalis (GNA) lectin which recognises terminal mannose sugars), and exist as active monomers of 52 kDa as determined by SDS-PAGE and by gel filtration. APase IA and IB have pH optima for p-nitrophenyl phosphate of 5.8 and 6.2, and pIs of 7.3 and 6.5, respectively. For APase II, both isoforms exist as active monomers of 113 kDa by SDS-PAGE and 92 kDa by gel filtration, with pH optima of 5.8 and 6.8, and pIs of 4.4 and 5.2 to 5.3 for IIA and IIB, respectively. Isoform IIA was not recognised by the two glycan probes, while IIB was recognised by mAb 2.23. The activity of all four isoforms was severely inhibited by Cu²⁺, Zn²⁺ and Mo²⁺, while each showed activity against a range of phosphate monoester substrates with highest substrate specificity (V_max/K_m) for ATP and PPi. Activity associated with APase I and II is detectable in roots isolated from plants maintained in P-containing media, but the activity of both is increased with the onset of P-deficiency. However, a temporal difference in response between APase I and II is observed over a 28-d time course of P-deprivation.     

Metal complexes with the ligand derived from 6-acetyl-1,3,7-trimethyllumazine and benzohydrazide. Molecular structures of two new Co(II) and Rh(III) complexes and analysis of in vitro antitumor activity

The structures and spectroscopic properties of new Mn(II), Co(II), Cd(II), Hg(II), Ag(I), Rh(III), and Ir(I) complexes with the ligand BZLMH derived from 6-acetyl-1,3,7-trimethyllumazine (lumazine = pteridine-2,4(1H,3H)-dione) and benzohydrazide are reported. Complexes have been characterized by elemental analyses, spectroscopic studies (IR, UV-vis, ¹H, ¹³C and ¹⁵N NMR) and magnetic measurements. In all the complexes, the lumazine-derived ligand appears to be coordinated in either tridentate (N5, N61 and O63) or tetradentate forms (O4, N5, N61 and O63). The molecular structures of the [Co(BZLMH)(H₂O)(CH₃CN)₂](ClO₄)₂ · CH₃CN and [RhCl₂(BZLM)(CH₃CN)] · CH₃CN complexes, determined by single crystal X-ray diffraction, have allowed to corroborate both coordination behaviours.The cytotoxic activity of the free ligand and complexes against human neuroblastoma NB69 cell line is also described. The differential analysis of the initial cytotoxic screening data has shown good activity only for the [RhCl₂(BZLM)(CH₃CN)] · CH₃CN compound at concentrations at around 2 μM; for the other complexes, a modulation of the cell growth was not found upon complexation, this non-specific effect strongly suggesting an apoptotic behaviour.     

Preparation of Site-Specific Isotopically Labelled Zervamicins,the Antibiotic Peptaibols Produced by Emericellopsis Salmosynnemata

A simple procedure for the preparation of the specifically labelled peptide antibiotic zervamicins IC, IIA and IIB has been developed. The zervamicin molecules are labelled with stable isotopes by culturing the Emericellopsis salmosynnemata on a well-defined synthetic medium containing the highly isotopically enriched amino acid. To obtain the peptide with the specifically and highly enriched amino acid residue, precautions have been taken to prevent any de novo biosynthesis of the particular amino acid from unlabelled precursors. The enrichment of the labelled peptide is determined by mass spectrometric analysis. Following this method we have incorporated [2′,4′, 5′,6′,7′-²H₅]-L -Trp-1, [1′-¹⁵N]-L -Trp-1 and [2′, 3′,4′,5′,6′-²H₅]-L - Phl-16 into zervamicins IC, IIA and IIB on the preparative scale and without scrambling of the label. Thus, using the procedures described, isotopically labelled zervamicins can be prepared, allowing them to be studied by solid- state NMR.     

Characterization of a murine type IIB procollagen-specific antibody

Type II collagen is the major collagenous component of the cartilage extracellular matrix; formation of a covalently cross-linked type II collagen network provides cartilage with important tensile properties. The Col2a1 gene is encoded by 54 exons, of which exon 2 is subject to alternative splicing, resulting in different isoforms named IIA, IIB, IIC and IID. The two major procollagen protein isoforms are type IIA and type IIB procollagen. Type IIA procollagen mRNA contains exon 2 and is generated predominantly by chondroprogenitor cells and other non-cartilaginous tissues. Differentiated chondrocytes generate type IIB procollagen, devoid of exon 2. Although type IIA procollagen is produced in certain non-collagenous tissues during development, this developmentally-regulated alternative splicing switch to type IIB procollagen is restricted to cartilage cells. Though a much studied and characterized molecule, the importance of the various type II collagen protein isoforms in cartilage development and homeostasis is still not completely understood. Effective antibodies against specific epitopes of these isoforms can be useful tools to decipher function. However, most type II collagen antibodies to date recognize either all isoforms or the IIA procollagen isoform. To specifically identify the murine type IIB procollagen, we have generated a rabbit antibody (termed IIBN) directed to a peptide sequence that spans the murine exon 1–3 peptide junction. Characterization of the affinity-purified antibody by western blotting of collagens extracted from wild type murine cartilage or cartilage from Col2a1^+ ex2 knock-in mice (which generates predominantly the type IIA procollagen isoform) demonstrated that the IIBN antibody is specific to the type IIB procollagen isoform. IIBN antibody was also able to detect the native type IIB procollagen in the hypertrophic chondrocytes of the wild type growth plate, but not in those of the Col2a1^+ ex2 homozygous knock-in mice, by both immunofluorescence and immunohistochemical studies. Thus the IIBN antibody will permit an in-depth characterization of the distribution of IIB procollagen isoform in mouse skeletal tissues. In addition, this antibody will be an important reagent for characterizing mutant type II collagen phenotypes and for monitoring type II procollagen processing and trafficking.     

Synthesis and solvent dependency study of a novel iron complex with mono-cyanide and mono-carbonyl coordination

A novel iron complex [(1,5,8,12-tetraazadodecane)-cyano-iron carbonyl] (1), in which the iron center is coordinated with one cyanide (CN) and one carbonyl (CO), was synthesized. 1’s X-ray crystallographic structure was determined. The structure shows that cyanide and carbonyl are in the cis-isomeric position. Further infrared study of 1 in a DMF/H₂O system has shown that the both CN and CO stretching frequencies are very sensitive to the hydrogen bonding ability of the solvent system.     

DNA topoisomerase VIII: a novel subfamily of type IIB topoisomerases encoded by free or integrated plasmids in Archaea and Bacteria

Type II DNA topoisomerases are divided into two families, IIA and IIB. Types IIA and IIB enzymes share homologous B subunits encompassing the ATP-binding site, but have non-homologous A subunits catalyzing DNA cleavage. Type IIA topoisomerases are ubiquitous in Bacteria and Eukarya, whereas members of the IIB family are mostly present in Archaea and plants. Here, we report the detection of genes encoding type IIB enzymes in which the A and B subunits are fused into a single polypeptide. These proteins are encoded in several bacterial genomes, two bacterial plasmids and one archaeal plasmid. They form a monophyletic group that is very divergent from archaeal and eukaryotic type IIB enzymes (DNA topoisomerase VI). We propose to classify them into a new subfamily, denoted DNA topoisomerase VIII. Bacterial genes encoding a topoisomerase VIII are present within integrated mobile elements, most likely derived from conjugative plasmids. Purified topoisomerase VIII encoded by the plasmid pPPM1a from Paenibacillus polymyxa M1 had ATP-dependent relaxation and decatenation activities. In contrast, the enzyme encoded by mobile elements integrated into the genome of Ammonifex degensii exhibited DNA cleavage activity producing a full-length linear plasmid and that from Microscilla marina exhibited ATP-independent relaxation activity. Topoisomerases VIII, the smallest known type IIB enzymes, could be new promising models for structural and mechanistic studies.     

Using Group II Introns for Attenuating the In Vitro and In Vivo Expression of a Homing Endonuclease

In Chaetomium thermophilum (DSM 1495) within the mitochondrial DNA (mtDNA) small ribosomal subunit (rns) gene a group IIA1 intron interrupts an open reading frame (ORF) encoded within a group I intron (mS1247). This arrangement offers the opportunity to examine if the nested group II intron could be utilized as a regulatory element for the expression of the homing endonuclease (HEase). Constructs were generated where the codon-optimized ORF was interrupted with either the native group IIA1 intron or a group IIB type intron. This study showed that the expression of the HEase (in vivo) in Escherichia coli can be regulated by manipulating the splicing efficiency of the HEase ORF-embedded group II introns. Exogenous magnesium chloride (MgCl₂) stimulated the expression of a functional HEase but the addition of cobalt chloride (CoCl₂) to growth media antagonized the expression of HEase activity. Ultimately the ability to attenuate HEase activity might be useful in precision genome engineering, minimizing off target activities, or where pathways have to be altered during a specific growth phase.     

Improving the hydrogen storage properties of metal-organic framework by functionalization

Based on the structure of MOF-808, different substituents were introduced to replace hydrogen atom on the phenyl ring of MOF-808. The GCMC method was used to study the effect of functional groups on the hydrogen storage properties of MOF-808-X (X?=??OH, ?NO₂, ?CH₃, ?CN, ?I). The H₂ uptakes and isosteric heat of adsorption were simulated at 77 K. The results indicate that all these substituents have favorable impact on the hydrogen storage capacity, and –CN is found to be the most promising substituent to improve H₂ uptake. These results may be helpful for the design of MOFs with higher hydrogen storage capacity.

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Graphical abstract Atomistic structures of MOFs. (a) The structures of MOF-808-X. (b) Model of organic linker. Atom color scheme: C, gray; H, white; O, red; X, palegreen (X?=??OH, ?NO₂, ?CH₃, ?CN, ?I)

     

Hydrogen peroxide in artificial photosynthesizing systems

From the point of view of the concepts of hydrogen peroxide as a source of photosynthetic oxygen (hydrogen) coordination and photochemical properties of chlorophyll and its aggregates towards hydrogen peroxide were considered. The binding energy of H₂O and H₂O₂ with chlorophyll and chlorophyllide depending on their form (monomers, dimers and trimers) was estimated by quantum chemical calculations. It is shown that at an increase of the degree of the pigment aggregation binding energy of H₂O₂ was more than the energy of H₂O. Analysis of experimental results of the photochemical decomposition of hydrogen peroxide using chlorophyll was carried out. Estimates of the thermodynamic parameters (ΔG° and ΔH°) of the formation of organic compounds from CO₂ with water and hydrogen peroxide were compared. The interaction of CO₂ with H₂O₂ requires much less energy consumption than with water for all considered cases. The formation of organic products (formaldehyde, alcohols, carboxylic and carbonylic compounds) and simultaneous production of O₂ under the influence of visible light in the systems of inorganic carbon-hydrogen peroxide - chlorophyll (phthalocyanine) is detected by GC/MS method, FTIR spectroscopy, and chemical analysis.     

Enhanced removability of odorous sulfur-containing gases by mixed cultures of purified bacteria from peat biofilters

Four bacteria isolated from peat biofilters, Thiobacillus thioparus DW44, Thiobacillus sp. HA43, Xanthomonas sp. DY44 and Hyphomicrobium sp. I55, were selected to enhance the removal ratios of hydrogen sulfide (H₂S), methanethiol (MT) and dimethyl sulfide (DMS) in a mixed gas system. Two bacteria, DW44 and I55, which degrade H₂S, MT, DMS and dimethyl disulfide (DMDS), were mixed with DY44 or HA43 which degrade only H₂S and MT. Although DMS removal was significantly inhibited by the presence of H₂S and MT in a peat biofilter inoculated with the single bacterium, enhanced removability of H₂S, MT and DMS was observed by mixing Hyphomicrobium sp. I55 either with Thiobacillus sp. HA43 or Xanthomonas sp. DY44. The removal rate (g-S-kg-dry peat⁻¹·d⁻¹) by I55 after 8 d was 0.664 in total sulfur load, 0.827 g-S·kg-dry g-S·-kg-dry peat⁻¹·d⁻¹, but the rates by the mixed cultures of I55 plus HA43, and I55 plus DY44 were 0.760 and 0.801, respectively. In particular, DMS removability in mixed gases by a mixed culture of I55 and DY44 was almost equivalent to that by I55 when only DMS was supplied, suggesting that removal of H₂S and MT, which inhibited DMS removal, was preferentially conducted by DY44 and led to improved DMS removability by I55.     

Reactions of rhodium(II) and iridium(III) complexes bearing a P,O-coordination with tetracyanoethylene in the presence of KPF6

Reactions of Cp*M(MDMPP-P,O)Cl (1a: M=Rh, 1b: M=Ir; MDMPP-P,O=PPh₂(2-O-6-MeOC₆H₃)) with tetracyanoethylene (tcne) in the presence of KPF₆ gave Cp*MCl[PPh₂{2-O-3-(C(CN)₂CH(CN)₂)-6-MeOC₆H₂}] (2), [{Cp*MPPh₂{2-O-3-(C(CN)C(CN)₂)-6-MeOC₆H₂}}₂(CN)](PF₆) (3), [{Cp*IrPPh₂{2-O-3-(C(CN)C(CN)₂)-6-MeOC₆H₂}}(CN){Cp*Ir(MDMPP-P,O)}](PF₆) (4b) and [{Cp*Ir(MDMPP-P,O)}₂(CN)](PF₆) (5b), depending on the reaction conditions. Reaction of 2 with KPF₆ or AgOTf in the absence and presence of xylyl isocyanide (XylNC) gave 3 or [Cp*MCl{PPh₂(2-O-3-(C(CN)₂-CH(CN)₂)-6-MeOC₆H₂)}(XylNC)](OTf) (6). The structure of 3a (M=Rh) was confirmed by X-ray crystal analysis.     

Supramolecular assemblies of new 2-D complexes: Syntheses, crystal structures, spectroscopic and magnetic properties of {[MnAu2(CN)4(NITpPy)2(H2O)2]}n and {[Co(N(CN)2)2(NITpPy)2(H2O)2]}n

Two new complexes, {[MnAu₂(CN)₄(NITpPy)₂(H₂O)₂]}_n (1) and {[Co(N(CN)₂)₂(NITpPy)₂(H₂O)₂]}_n (2), have been synthesized and characterized. The single-crystal X-ray analysis for the complexes 1 and 2 demonstrates that each M(II) (M = Mn or Co) ion assumes a distorted octahedral MN₄O₂ coordination polyhedron. Four nitrogen atoms come from the cyanide groups and the pyridyl rings in a common plane, and two oxygen atoms come from the H₂O molecules in trans-positions. The structures of complexes 1 and 2 illustrate that aurophilicity and/or hydrogen bonding interactions play important roles in increasing dimensionality. Magnetic investigations on complexes 1 and 2 show the presence of weak antiferromagnetic interactions.     

Nitrite,sodium nitroprusside,potassium ferricyanide and hydrogen peroxide release dormancy of <Emphasis Type="Italic">Amaranthus retroflexus</Emphasis> seeds in a nitric oxide-dependent manner

Nitric oxide (NO) and reactive oxygen species (ROS) are important regulators involving various processes of plant growth and development. Amaranthus retroflexus L. seeds possess a relative dormancy property that means freshly collected seeds can only germinate over a limited, high temperature range. Here, we show that the relative dormancy of A. retroflexus seeds could be significantly released following treatments with exogenous NO/cyanide (CN) donors such as nitrite, gases evolved from acidified nitrite, sodium nitroprusside (SNP), potassium ferricyanide (Fe(III)CN) and gases evolved from SNP or Fe(III)CN solutions, as well as exogenously supplied ROS, hydrogen peroxide (H₂O₂). However, the effectiveness varied among these chemicals. Gases evolved from acidified nitrite displayed maximum effect while H₂O₂ had minimum effect. We also show that the effects of these compounds could be significantly inhibited by NO specific scavenger 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl 3-oxide (PTIO), indicating that NO signaling pathway might play a central role in the dormancy release and germination of A. retroflexus seeds, while both ROS and CN might act through NO-dependent signaling cascades.     

Metal ions-nucleobases interactions: preparation and crystal structures of trichloroadeninium zinc(ii)(form ii) and a similar zinc complex of arprinocid [6-amino-9-(2-chloro-6-fluorobenzyl)purine]

Two zinc complexes—trichloroadeninium zinc(II)(Form 11), C₅H₆N₅Cl₃Zn [structure(I)] and a similar complex of Arprinocid, (6-amino-9-(2-chloro-6-fluorobenzyl)purine], C₁₂H₁₀N₅FCl₄Zn [structure(II)]—have been prepared Structure(I) crystallizes in the space group P2₁/c with a = 8.223(1)Å, b = 6.755(1) Å, c = 18.698(3) Å, β = 96.10(2)°,and Z = 4. Structure(II) crystallizes in the space group P2₁/c with a = 8.209(2) Å, b = 6.421(8) Å, c = 31.794(8) Å, β = 90.76(2)°, and Z = 4. Both of these structures were solved by the heavy atom method using diffractometric data and refined to R = 0.028 [structure(I)] and 0.038 [structure(II)]. Zinc with a distorted tetrahedral coordination having three chlorines and N(7) as ligators, protonation of the adenine moiety at N(1), dissymmetry of exocyclic angles at N(7), and an interligand hydrogen bond (“indirect chelation”) involving one of the three chlorines, coordinated to zinc and a proton of the exocylic amino group are the striking features common to both structures. Similar types of indirect chelation as observed in the different complexes of purines have been discussed. The zinc ion deviates from the imidazole plane by 0.412 Å in structure(I) and 0.524 Å in Structure(II). The imidazol and pyrimidine planes fold about the C(4)-C(5) bond by 2.4° in strctur(I) and 3.8° in structure(II). In structure(I), inversion related molecules are paired through N(9)-H…N(3) hydrogen bonds. N-H…Cl hydrogen bonds and C(8)-H…Cl interactions have been observed in both structures.     

f-Element/crown ether complexes. 16. Synthesis,crystallization and crystal structure of [Dy(OH2)8]Cl3·18-crown-6·4H2O

When crystals of [Dy(OH₂)₇(OHMe)] [DyCl(OH₂)₂(18- crown-6)]₂Cl₇·2H₂O [1] are allowed to warm from 5 °C to ambient temperature (22 °C) under the original solvent mixture (1:3 CH₃OH: CH₃CN), they redissolve and the title complex can be isolated by slow evaporation of the resulting solution. The crystal structure of this complex, [Dy(OH₂)₈]Cl₃·18-crown-₆·4H₂O, has been determined. It crystallizes in the monoclinic space group, P2₁/c, with a = 10.395(1), b = 18.684(1), c = 16.259- (3) Å, β= 102.56(1)°, and D_calc = 1.61 g cm⁻³ for Z = 4. A final conventional R value of 0.041 was obtained by least-squares refinement using 3453 independent observed [F_o⩾5σ(F_o)] reflections. The [Dy(OH₂)₈]³⁺ cations and crown ether molecules are hydrogen bonded in a polymeric chain with the crown molecules separating the cations and a total of seven DyOH₂···O(crown ether) hydrogen bonds. The chains are connected by a hydrogen bonding network consisting of the cations, chloride ions, and uncoordinated water molecules. The geometry of the cation is best described as a bicapped trigonal prism with distortions on the reaction pathway toward dodecahedral symmetry. The two capping atoms average 2.41(1) Å from Dy, the remaining DyO distances average 2.38(2) Å. The 18-crown-6 molecule has the D_3d conformation normally observed except for a distortion of one OCCO unit containing the oxygen atom accepting two hydrogen bonds.     

Photoproduction of hydrogen by photosystem I of Scenedesmus

Summary Anaerobically adapted and illuminated Scenedesmus evolves molecular hydrogen from endogenous organic compounds. This photoproduction of H₂ does not require photosystem II, since 5x10^-6 M DCMU, which inhibited normal photosynthesis almost completely, did not significantly inhibit the photoevolution of H₂. The relative efficiencies in far-red light of photosynthesis, photoreduction and H₂ production were determined. Photohydrogen evolution was comparatively the most efficient of these three processes. Three mutants of Scenedesmus (isolated and characterized by Dr. N. I. Bishop) were also tested. Mutant PS-50, which lacks cytochrome 552, did not photoproduce H₂. Mutant No. 11, blocked in photosystem II, showed rates of H₂ production comparable to those of the wild type. Cl-CCP, an uncoupler of photophosphorylation, caused an apparent stimulation of H₂ production by mutant No. 11 and wild-type cells. Mutant No. 8, which is partially blocked in photosystem I, showed a diminished photohydrogen production which was inhibited by Cl-CCP. These results suggest that photoproduction of hydrogen by photosystem I is due either to cyclic photophosphorylation, which supplies energy needed for a dark, H₂-yielding reaction, or to a more direct photooxidation of organic compounds by the photosynthetic electron transfer chain.The following abbreviations were used: Cl-CCP=carbonyl cyanide m-chlorophenylhydrazone; DCMU=3-(3,4-dichlorophenyl)-1,1-dimethylurea.This work was supported by contract AT-(40-1)-2687 from the U.S. Atomic Energy Commission to Professor H. Gaffron.     

Lactate dehydrogenase isozymes in type I,IIA and IIB fibres of rabbit skeletal muscles

Summary Lactate dehydrogenase (LDH) isozyme patterns were analysed by polyacrylamide (PAA) slab gel electrophoresis in extracts prepared from various rabbit skeletal muscles of defined fibre composition and by PAA microelectrophoresis of microdissected, histochemically typed single muscle fibres. The results obtained by electrophoresis of whole muscle extracts generally agreed with the data obtained from single fibre electrophoresis, i.e. the LDH isozyme pattern corresponded to that of the predominant fibre type. Type I Fibres from soleus and semitendinosus muscles were characterized by a unique pattern of all 5 LDH isozymes with a predominance of LDH-1, 2 and 3. The major fraction (80%) of the type II fibres from extensor digitorum longus and tibialis anterior muscles contained only LDH-5 (M₄). About 20% of the type II fibres contained in addition to LDH-5 small amounts of LDH-4 and LDH-3. The fraction of fibres containing LDH-5, LDH-4, and LDH-3 was similar (ca. 20%) in the histochemically defined IIA and IIB subpopulations In view of the fact that the major fractions of rabbit IIB fibres display low and of IIA fibres high aerobic oxidative capacities (Reichmann and Pette 1982), these data indicate that the expression of the H-subunit of LDH is not correlated with the aerobic-oxidative capacity of the fibre. It also appears not to be correlated with the presence of different myosin isoforms in IIA and IIB fibres.     

Photosystem I light-harvesting proteins regulate photosynthetic electron transfer and hydrogen production

Linear electron flow (LEF) and cyclic electron flow (CEF) compete for light-driven electrons transferred from the acceptor side of photosystem I (PSI). Under anoxic conditions, such highly reducing electrons also could be used for hydrogen (H₂) production via electron transfer between ferredoxin and hydrogenase in the green alga Chlamydomonas reinhardtii. Partitioning between LEF and CEF is regulated through PROTON-GRADIENT REGULATION5 (PGR5). There is evidence that partitioning of electrons also could be mediated via PSI remodeling processes. This plasticity is linked to the dynamics of PSI-associated light-harvesting proteins (LHCAs) LHCA2 and LHCA9. These two unique light-harvesting proteins are distinct from all other LHCAs because they are loosely bound at the PSAL pole. Here, we investigated photosynthetic electron transfer and H₂ production in single, double, and triple mutants deficient in PGR5, LHCA2, and LHCA9. Our data indicate that lhca2 and lhca9 mutants are efficient in photosynthetic electron transfer, that LHCA2 impacts the pgr5 phenotype, and that pgr5/lhca2 is a potent H₂ photo-producer. In addition, pgr5/lhca2 and pgr5/lhca9 mutants displayed substantially different H₂ photo-production kinetics. This indicates that the absence of LHCA2 or LHCA9 impacts H₂ photo-production independently, despite both being attached at the PSAL pole, pointing to distinct regulatory capacities.

Alteration of the light-harvesting composition of photosystem I impacts photosynthetic electron transfer and hydrogen production.     

Effect of ethylene and carbon dioxide on potato metabolism: stimulation of tuber and mitochondrial respiration, and inducement of the alternative path

The respiration of potato tubers (Solanum tuberosum var. Russet Burbank) which have been kept at room temperature for 10 days is stimulated upon subsequent treatment with C₂H₄ (10 microliters per liter) and O₂. The respiratory rise reaches a peak in 24 to 30 hours and thereafter declines. Coincident with the rise in tuber respiration is an increase in the respiratory rates of fresh slices and isolated mitochondria. Slices and mitochondria from C₂H₄- and O₂-treated tubers also display substantial resistance to CN, and the resistant respiration is inhibited by hydroxamates.

The longer the tubers are stored after harvest, the less effective is C₂H₄ in causing CN resistance in slices and mitochondria from treated tubers. Addition of 10% CO₂ to the C₂H₄-O₂ mixture, however, causes extensive CN resistance to develop, even in slices and mitochondria from old tubers. The results show that C₂H₄, O₂, and CO₂ act synergistically to induce alternative path development in potatoes.