NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina

Miguel Pessanha; David L Turner; Emma L Rothery; Katherine L Pankhurst; Graeme A Reid; Stephen K Chapman; Antonio V Xavier; Carlos A Salgueiro

doi:10.1016/S0020-1693(03)00179-8

NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina

Miguel Pessanha, David L Turner, Emma L Rothery, Katherine L Pankhurst, Graeme A Reid, Stephen K Chapman, Antonio V Xavier, Carlos A Salgueiro

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages. (C) 2003 Elsevier Science B.V. All rights reserved.

Original language	English
Pages (from-to)	379-381
Number of pages	3
Journal	Inorganica Chimica Acta
Volume	356
DOIs	https://doi.org/10.1016/S0020-1693(03)00179-8
Publication status	Published - 3 Dec 2003

Keywords

ENERGY TRANSDUCTION
paramagnetic shifts
DESULFOVIBRIO-VULGARIS
multihaem
RESPIRATION
Shewanella
electron tranfer protein
PUTREFACIENS MR-1
ELECTRON-TRANSFER
COOPERATIVITY
flavocytochrome
NCIMB400
NMR
FUMARATE REDUCTASE
CYTOCHROME C(3)
HEME CORE

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@article{4d7223f8ae064fadb1bcff63f0d35db1,

title = "NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina",

abstract = "Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages. (C) 2003 Elsevier Science B.V. All rights reserved.",

keywords = "ENERGY TRANSDUCTION, paramagnetic shifts, DESULFOVIBRIO-VULGARIS, multihaem, RESPIRATION, Shewanella, electron tranfer protein, PUTREFACIENS MR-1, ELECTRON-TRANSFER, COOPERATIVITY, flavocytochrome, NCIMB400, NMR, FUMARATE REDUCTASE, CYTOCHROME C(3), HEME CORE",

author = "Miguel Pessanha and Turner, {David L} and Rothery, {Emma L} and Pankhurst, {Katherine L} and Reid, {Graeme A} and Chapman, {Stephen K} and Xavier, {Antonio V} and Salgueiro, {Carlos A}",

year = "2003",

month = dec,

day = "3",

doi = "10.1016/S0020-1693(03)00179-8",

language = "English",

volume = "356",

pages = "379--381",

journal = "Inorganica Chimica Acta",

issn = "0020-1693",

publisher = "Elsevier",

}

TY - JOUR

T1 - NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina

AU - Pessanha, Miguel

AU - Turner, David L

AU - Rothery, Emma L

AU - Pankhurst, Katherine L

AU - Reid, Graeme A

AU - Chapman, Stephen K

AU - Xavier, Antonio V

AU - Salgueiro, Carlos A

PY - 2003/12/3

Y1 - 2003/12/3

N2 - Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages. (C) 2003 Elsevier Science B.V. All rights reserved.

AB - Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages. (C) 2003 Elsevier Science B.V. All rights reserved.

KW - ENERGY TRANSDUCTION

KW - paramagnetic shifts

KW - DESULFOVIBRIO-VULGARIS

KW - multihaem

KW - RESPIRATION

KW - Shewanella

KW - electron tranfer protein

KW - PUTREFACIENS MR-1

KW - ELECTRON-TRANSFER

KW - COOPERATIVITY

KW - flavocytochrome

KW - NCIMB400

KW - NMR

KW - FUMARATE REDUCTASE

KW - CYTOCHROME C(3)

KW - HEME CORE

U2 - 10.1016/S0020-1693(03)00179-8

DO - 10.1016/S0020-1693(03)00179-8

M3 - Article

VL - 356

SP - 379

EP - 381

JO - Inorganica Chimica Acta

JF - Inorganica Chimica Acta

SN - 0020-1693

ER -

NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina

Abstract

Keywords

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