1gm4
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(New page: 200px<br /> <applet load="1gm4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gm4, resolution 2.05Å" /> '''OXIDISED STRUCTURE ...)
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Revision as of 16:38, 29 October 2007
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OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6
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, ... [(full description)]
About this Structure
1GM4 is a [Single protein] structure of sequence from [Desulfovibrio desulfuricans] with SO4 and HEC as [ligands]. Full crystallographic information is available from [OCA].
Reference
Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome., Louro RO, Bento I, Matias PM, Catarino T, Baptista AM, Soares CM, Carrondo MA, Turner DL, Xavier AV, J Biol Chem. 2001 Nov 23;276(47):44044-51. Epub 2001 Sep 10. PMID:11551953
Page seeded by OCA on Mon Oct 29 18:43:21 2007
