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1w7o

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{{STRUCTURE_1w7o| PDB=1w7o | SCENE= }}
{{STRUCTURE_1w7o| PDB=1w7o | SCENE= }}
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'''CYTOCHROME C3 FROM DESULFOMICROBIUM BACULATUS'''
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===CYTOCHROME C3 FROM DESULFOMICROBIUM BACULATUS===
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==Overview==
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The tetraheme cytochrome c3 isolated from Desulfomicrobium baculatum (DSM 1743)(Dsmb) was cloned, and the sequence analysis showed that this cytochrome differs in just three amino acid residues from the cytochrome c3 isolated from Desulfomicrobium norvegicum (Dsmn): (DsmnXXDsmb) Thr-37 --&gt; Ser, Val-45 --&gt; Ala, and Phe-88 --&gt; Tyr. X-ray crystallography was used to determine the structure of cytochrome c3 from Dsmb, showing that it is very similar to the published structure of cytochrome c3 from Dsmn. A detailed thermodynamic and kinetic characterization of these two tetraheme cytochromes c3 was performed by using NMR and visible spectroscopy. The results obtained show that the network of cooperativities between the redox and protonic centers is consistent with a synergetic process to stimulate the hydrogen uptake activity of hydrogenase. This is achieved by increasing the affinity of the cytochrome for protons through binding electrons and, reciprocally, by favoring a concerted two-electron transfer assisted by the binding of proton(s). The data were analyzed within the framework of the differences in the primary and tertiary structures of the two proteins, showing that residue 88, close to heme I, is the main cause for the differences in the microscopic thermodynamic parameters obtained for these two cytochromes c3. This comparison reveals how replacement of a single amino acid can tune the functional properties of energy-transducing proteins, so that they can be optimized to suit the bioenergetic constraints of specific habitats.
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==About this Structure==
==About this Structure==
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[[Category: Electron transport]]
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Revision as of 09:23, 28 July 2008

Image:1w7o.png

Template:STRUCTURE 1w7o

CYTOCHROME C3 FROM DESULFOMICROBIUM BACULATUS

Template:ABSTRACT PUBMED 15456779

About this Structure

1W7O is a Single protein structure of sequence from Desulfomicrobium baculatum. Full crystallographic information is available from OCA.

Reference

Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp., Correia IJ, Paquete CM, Coelho A, Almeida CC, Catarino T, Louro RO, Frazao C, Saraiva LM, Carrondo MA, Turner DL, Xavier AV, J Biol Chem. 2004 Dec 10;279(50):52227-37. Epub 2004 Sep 28. PMID:15456779

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