1gm4: Difference between revisions

Revision as of 05:30, 1 July 2008

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File:1gm4.png

Template:STRUCTURE 1gm4

OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6

Template:ABSTRACT PUBMED 11551953

About this StructureAbout this Structure

1GM4 is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6'''
+===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 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11551953}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11551953}}
 ==About this Structure==
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 [[Category: Cytochrome]]
 [[Category: Electron transport]]
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