1w7o
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The tetraheme cytochrome c3 isolated from Desulfomicrobium baculatum (DSM | + | 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 --> Ser, Val-45 --> Ala, and Phe-88 --> 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Desulfomicrobium baculatum]] | [[Category: Desulfomicrobium baculatum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carrondo, M | + | [[Category: Carrondo, M A.]] |
| - | [[Category: Coelho, A | + | [[Category: Coelho, A V.]] |
[[Category: Frazao, C.]] | [[Category: Frazao, C.]] | ||
| - | [[Category: Matias, P | + | [[Category: Matias, P M.]] |
[[Category: HEC]] | [[Category: HEC]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
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[[Category: redox-bohr effect]] | [[Category: redox-bohr effect]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:20 2008'' |
Revision as of 13:41, 21 February 2008
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CYTOCHROME C3 FROM DESULFOMICROBIUM BACULATUS
Overview
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 --> Ser, Val-45 --> Ala, and Phe-88 --> 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.
About this Structure
1W7O is a Single protein structure of sequence from Desulfomicrobium baculatum with as ligand. Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 15:41:20 2008
