1gm4: Difference between revisions
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==Overview== | ==Overview== | ||
Cell metabolism relies on energy transduction usually performed by complex, membrane-spanning proteins that couple different chemical processes, e.g., electron and proton transfer in proton-pumps. There is great interest in, determining at the molecular level the structural details that control, these energy transduction events, particularly those involving multiple, electrons and protons, because tight control is required to avoid the, production of dangerous reactive intermediates. Tetraheme cytochrome c(3), is a small soluble and monomeric protein that performs a central step in, the bioenergetic metabolism of sulfate reducing bacteria, termed, "proton-thrusting," linking the oxidation of molecular hydrogen with the, reduction of sulfate. The mechano-chemical coupling involved in the, ... | Cell metabolism relies on energy transduction usually performed by complex, membrane-spanning proteins that couple different chemical processes, e.g., electron and proton transfer in proton-pumps. There is great interest in, determining at the molecular level the structural details that control, these energy transduction events, particularly those involving multiple, electrons and protons, because tight control is required to avoid the, production of dangerous reactive intermediates. Tetraheme cytochrome c(3), is a small soluble and monomeric protein that performs a central step in, the bioenergetic metabolism of sulfate reducing bacteria, termed, "proton-thrusting," linking the oxidation of molecular hydrogen with the, reduction of sulfate. The mechano-chemical coupling involved in the, transfer of multiple electrons and protons in cytochrome c(3) from, Desulfovibrio desulfuricans ATCC 27774 is described using results derived, from the microscopic thermodynamic characterization of the redox and, acid-base centers involved, crystallographic studies in the oxidized and, reduced states of the cytochrome, and theoretical studies of the redox and, acid-base transitions. This proton-assisted two-electron step involves, very small, localized structural changes that are sufficient to generate, the complex network of functional cooperativities leading to energy, transduction, while using molecular mechanisms distinct from those, established for other Desulfovibrio sp. cytochromes from the same, structural family. | ||
==About this Structure== | ==About this Structure== | ||
1GM4 is a | 1GM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with SO4 and HEC as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GM4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:41:01 2007'' | ||
