Spectroscopical and functional characterization of the hemoglobin of Nostoc commune UTEX 584 (Cyanobacteria) |
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| Affiliation: | 1. Department of Biochemistry and Anaerobic Microbiology, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA;2. Zoophysiology Department, Aarhus University, 8000 Aarhus C, Denmark;1. Division of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia;2. Division of Molecular Medicine, Ruđer Bošković Institute, Zagreb, Croatia;3. Dipartimento di Medicina Clinica e Chirurgia, Universita'' degli Studi di Napoli Federico II, Napoli, Italy;4. Laboratory for Medical Biochemistry, Tomislav Bardek General Hospital, Koprivnica, Croatia;1. Department of Infection and Immunity, Experimental and Molecular Immunology, Luxembourg Institute of Health, 29, rue Henri Koch, L-4354 Esch-sur-Alzette, Luxembourg;2. Department of Infection and Immunity, Immune Systems Biology, Luxembourg Institute of Health, 29, rue Henri Koch, L-4354 Esch-sur-Alzette, Luxembourg;3. Odense Research Center for Anaphylaxis (ORCA), Department of Dermatology and Allergy Center, Odense University Hospital, University of Southern Denmark, Odense, Denmark;1. Department of Chemical Engineering, Faculty of Engineering and Science, Curtin University Malaysia, CDT 250, 98009 Miri, Sarawak, Malaysia;2. Department of Mechanical Engineering, Faculty of Engineering and Science, Curtin University Malaysia, CDT 250, 98009 Miri, Sarawak, Malaysia;1. Department of Biochemistry and Molecular Biology, College of Medicine, University of South Alabama, Mobile, AL, 36688, United States;2. Department of Biotechnology, Korea National University of Transportation, Chungbuk, 27909, Republic of Korea;3. Mitchell Cancer Institute, University of South Alabama, Mobile, AL, 36604, United States |
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| Abstract: | Structural analysis of a monomeric hemoglobin from the cyanobacterium Nostoc commune strain UTEX 584, cyanoglobin (Potts et al. (1992) Science 256, 1690–1692), is presented. Cyanoglobin binds molecular oxygen reversibly, with high oxygen affinity and non-cooperativity. There was no evidence for decreased stability of the pigment at 37°C. Cyanoglobin-specific antibodies showed no cross-reactivity with two reference hemoglobins, leghemoglobin a and sperm whale myoglobin. The absorption spectral properties of cyanoglobin differ significantly from those of the two reference hemoglobins. The spectrum of oxy-cyanoglobin most closely resembles that of an oxy-hemoglobin from the protozoan Tetrahymena pyriformis, a hemoprotein that shares substantial amino-acid sequence identity with cyanoglobin. Met-cyanoglobin possesses spectral characteristics at pH 7.0–9.0 that resemble those of the alkaline met-hemoglobin (a putative hemichrome) of another protozoan, Paramecium caudatum. The spin-state character of met-cyanoglobin is pH-dependent. Met-cyanoglobin does not coordinate the strong-field ligands, cyanide and azide, at pH 7.0. The capacity of cyanoglobin to coordinate cyanide increased with decreasing pH. Far-UV CD spectra of cyanoglobin are indicative of a protein with a significant amount of alpha-helical structure. Data from Soret-region CD spectra suggest that the orientations of the heme moieties in cyanoglobin and leghemoglobin a are similar to one another. |
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