Complex formation between Chlorobium limicola f. thiosulfatophilumc-type cytochromes |
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| Institution: | 1. Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409 U.S.A.;2. Department of Biochemistry, University of Arizona, Tucson, AZ 85721 U.S.A.;1. MARE – Marine and Environmental Sciences Centre, Universidade de Lisboa, Faculdade de Ciências, Campo Grande, 1749-016 Lisboa, Portugal;2. Centro de Biologia Marinha, Universidade de São Paulo, Rod. Manoel Hipólito do Rego, km 131.5, São Sebastião, SP, Brazil;3. MARE – Marine and Environmental Sciences Centre, c/o Department of Zoology, Faculty of Sciences and Technology, University of Coimbra, 3000 Coimbra, Portugal;1. Department of Polymer Engineering, University of Akron, Akron, OH, 44325, USA;2. Departments of Materials and Mechanical Engineering, Purdue University, West Lafayette, IN, 47907, USA;1. Sa Tórtora 8, 17488 Cadaqués, Girona, Spain;2. Departament de Geologia, Universitat Autònoma de Barcelona, 08193 Bellaterra, Barcelona, Spain;1. College of Health and Life Sciences, Hamad Bin Khalifa University, Qatar Foundation, Doha, Qatar;2. Biological Sciences Program, Carnegie Mellon University in Qatar, Qatar;3. Division of Sustainable Development, College of Science and Engineering, Hamad Bin Khalifa University, Qatar Foundation, Doha, Qatar;1. Department of Life Sciences, Imperial College, Exhibition Road, London, SW7 2AZ, UK;2. Turkish Accelerator and Radiation Laboratory, Gölba??, 06830, Ankara, Turkiye;3. Cambrium GmbH, Max-Urich-Strasse 3, 13355, Berlin, Germany;1. Department of Chemical Engineering, Kyung Hee University, Gyeonggi-do, 17104, Republic of Korea;2. Department of Chemical and Biomolecular Engineering, Sogang University, Seoul, 04107, Republic of Korea |
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| Abstract: | It has been possible to demonstrate, using affinity chromatography, that Chlorobium flavocytochrome c-553 forms an electrostatically stabilized complex with Chlorobium cytochrome c-555. The binding site for cytochrome c-555 appears to be located on the heme-containing subunit of flavocytochrome c-553. This complex appears to be involved in the flavocytochrome c-553-catalyzed transfer of electrons from sulfide to cytochrome c-555. Complex formation has also been demonstrated between Chlorobium cytochromes c-555 and c-551, two components involved in the oxidation of thiosulfate by this green sulfur bacterium. Affinity chromatography data also suggest the possibility that the cytochrome binding sites on the Chlorobium flavocytochrome c-553 and on flavocytochrome c-552 from the purple sulfur bacterium Chromatium vinosum may be similar. |
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