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NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation

NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation
NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation
The tetrahaem cytochrome isolated during anaerobic growth of Shewanella frigidimarina NCIMB400 is a small protein (86 residues) involved in electron transfer to Fe(III), which can be used as a terminal respiratory oxidant by this bacterium. A 3D solution structure model of the reduced form of the cytochrome has been determined using NMR data in order to determine the relative orientation of the haems. The haem core architecture of S. frigidimarina tetrahaem cytochrome differs from that found in all small tetrahaem cytochromes c(3) so far isolated from strict anaerobes, but has some similarity to the N-terminal cytochrome domain of flavocytochrome c(3) isolated from the same bacterium. NMR signals obtained for the four haems of S. frigidimarina tetrahaem cytochrome at all stages of oxidation were cross-assigned to the solution structure using the complete network of chemical exchange connectivities. Thus, the order in which each haem in the structure becomes oxidised was determined.
multihaem cytochrome, nuclear magnetic resonance, ring current, iron-respiration, shewanelladesulfovibrio-vulgaris hildenborough, fumarate reductase, putrefaciensmr-1, desulfuricans atcc-27774, crystal-structure, proton thruster, c(3), redox, gigas, flavocytochrome
0014-5793
8-13
Pessanha, Miguel
7e563109-5e0f-4949-b0cc-9cab7a8e2809
Brennan, Lorraine
efa9251d-9605-48ae-b1b0-27129a4a9270
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228
Cuthbertson, Pauline M.
622e17ad-e1c0-42dc-b611-a3f5b0bc2180
Reid, Graeme A.
ff22c1ca-6493-43e5-9def-d46ae425eaf7
Chapman, Stephen K.
c8004be1-78bc-406c-8150-2cc282f910fa
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Salgueiro, Carlos A.
a9805ac9-e610-42ca-bb85-ef4e288eeffb
Pessanha, Miguel
7e563109-5e0f-4949-b0cc-9cab7a8e2809
Brennan, Lorraine
efa9251d-9605-48ae-b1b0-27129a4a9270
Xavier, António V.
77269a6a-27cb-4c75-abf0-7d03ac64c228
Cuthbertson, Pauline M.
622e17ad-e1c0-42dc-b611-a3f5b0bc2180
Reid, Graeme A.
ff22c1ca-6493-43e5-9def-d46ae425eaf7
Chapman, Stephen K.
c8004be1-78bc-406c-8150-2cc282f910fa
Turner, David L.
6c4c1ccb-a6f2-47cf-944e-e69269198a29
Salgueiro, Carlos A.
a9805ac9-e610-42ca-bb85-ef4e288eeffb

Pessanha, Miguel, Brennan, Lorraine, Xavier, António V., Cuthbertson, Pauline M., Reid, Graeme A., Chapman, Stephen K., Turner, David L. and Salgueiro, Carlos A. (2001) NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation. FEBS Letters, 489 (1), 8-13. (doi:10.1016/S0014-5793(00)02383-8).

Record type: Article

Abstract

The tetrahaem cytochrome isolated during anaerobic growth of Shewanella frigidimarina NCIMB400 is a small protein (86 residues) involved in electron transfer to Fe(III), which can be used as a terminal respiratory oxidant by this bacterium. A 3D solution structure model of the reduced form of the cytochrome has been determined using NMR data in order to determine the relative orientation of the haems. The haem core architecture of S. frigidimarina tetrahaem cytochrome differs from that found in all small tetrahaem cytochromes c(3) so far isolated from strict anaerobes, but has some similarity to the N-terminal cytochrome domain of flavocytochrome c(3) isolated from the same bacterium. NMR signals obtained for the four haems of S. frigidimarina tetrahaem cytochrome at all stages of oxidation were cross-assigned to the solution structure using the complete network of chemical exchange connectivities. Thus, the order in which each haem in the structure becomes oxidised was determined.

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More information

Published date: 26 January 2001
Keywords: multihaem cytochrome, nuclear magnetic resonance, ring current, iron-respiration, shewanelladesulfovibrio-vulgaris hildenborough, fumarate reductase, putrefaciensmr-1, desulfuricans atcc-27774, crystal-structure, proton thruster, c(3), redox, gigas, flavocytochrome

Identifiers

Local EPrints ID: 19594
URI: http://eprints.soton.ac.uk/id/eprint/19594
ISSN: 0014-5793
PURE UUID: 7698767b-9358-4fe8-9b4b-205d5461e8e6

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Date deposited: 14 Feb 2006
Last modified: 15 Jul 2019 19:27

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Contributors

Author: Miguel Pessanha
Author: Lorraine Brennan
Author: António V. Xavier
Author: Pauline M. Cuthbertson
Author: Graeme A. Reid
Author: Stephen K. Chapman
Author: David L. Turner
Author: Carlos A. Salgueiro

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