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Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp

Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp
Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp
The tetraheme cytochrome c(3) 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 c(3) 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 c(3) from Dsmb, showing that it is very similar to the published structure of cytochrome c(3) from Dsmn. A detailed thermodynamic and kinetic characterization of these two tetraheme cytochromes c(3) 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 c(3). 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.
desulfovibrio-vulgaris hildenborough, energy transduction, desulfuricans norway, electron-transfer, desulfuromonas-acetoxidans, angstrom resolution, redox potentials, structural basis, c-oxidase, 4hemes
0021-9258
52227-52237
Correia, Ilídio J.
7dc4bc5e-f872-4d39-a9db-0fc59dae4a26
Paquete, Catarina M.
505734a6-bb69-4243-be1e-b78df93870c2
Coelho, Ana
52ca6e84-c5fd-4006-8183-46afbf732677
Almeida, Claudia C.
a345dead-8ae8-4887-a95a-7229dd3979b8
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Frazão, Carlos
d20017c0-3587-446b-bc1e-879f79c69fa5
Saraiva, Lígia M.
a90fa967-526f-48b1-8640-62b9ddf4748c
Carrondo, Maria Arménia
26a04601-ce94-4cc9-a2f4-0d6a3c2ba544
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228
Correia, Ilídio J.
7dc4bc5e-f872-4d39-a9db-0fc59dae4a26
Paquete, Catarina M.
505734a6-bb69-4243-be1e-b78df93870c2
Coelho, Ana
52ca6e84-c5fd-4006-8183-46afbf732677
Almeida, Claudia C.
a345dead-8ae8-4887-a95a-7229dd3979b8
Catarino, Teresa
608a4400-1611-4798-bf27-7472e7c6a476
Louro, Ricardo O.
8014cf88-eb58-4ecd-8e04-8ce90a4e43f6
Frazão, Carlos
d20017c0-3587-446b-bc1e-879f79c69fa5
Saraiva, Lígia M.
a90fa967-526f-48b1-8640-62b9ddf4748c
Carrondo, Maria Arménia
26a04601-ce94-4cc9-a2f4-0d6a3c2ba544
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228

Correia, Ilídio J., Paquete, Catarina M., Coelho, Ana, Almeida, Claudia C., Catarino, Teresa, Louro, Ricardo O., Frazão, Carlos, Saraiva, Lígia M., Carrondo, Maria Arménia, Turner, David L. and Xavier, António V. (2004) Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp. The Journal of Biological Chemistry, 279 (50), 52227-52237. (doi:10.1074/jbc.M408763200).

Record type: Article

Abstract

The tetraheme cytochrome c(3) 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 c(3) 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 c(3) from Dsmb, showing that it is very similar to the published structure of cytochrome c(3) from Dsmn. A detailed thermodynamic and kinetic characterization of these two tetraheme cytochromes c(3) 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 c(3). 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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More information

Published date: 10 December 2004
Keywords: desulfovibrio-vulgaris hildenborough, energy transduction, desulfuricans norway, electron-transfer, desulfuromonas-acetoxidans, angstrom resolution, redox potentials, structural basis, c-oxidase, 4hemes

Identifiers

Local EPrints ID: 20174
URI: https://eprints.soton.ac.uk/id/eprint/20174
ISSN: 0021-9258
PURE UUID: 04bde7e3-744a-455b-861b-be7e4e054f70

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Date deposited: 22 Feb 2006
Last modified: 17 Jul 2017 16:29

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Contributors

Author: Ilídio J. Correia
Author: Catarina M. Paquete
Author: Ana Coelho
Author: Claudia C. Almeida
Author: Teresa Catarino
Author: Ricardo O. Louro
Author: Carlos Frazão
Author: Lígia M. Saraiva
Author: Maria Arménia Carrondo
Author: David L. Turner
Author: António V. Xavier

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