NMR redox studies of flavocytochrome c(3) from Shewanella frigidimarina

Pessanha, M., Turner, D. L., Rothery, E. L., Pankhurst, K. L., Reid, G. A., Chapman, S. K., Xavier, A. V. and Salgueiro, C. A. (2003) NMR redox studies of flavocytochrome c(3) from Shewanella frigidimarina Inorganica Chimica Acta, 356, pp. 379-381. (doi:10.1016/S0020-1693(03)00179-8).


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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.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1016/S0020-1693(03)00179-8
ISSNs: 0020-1693 (print)
Keywords: shewanella, electron tranfer protein, multihaem, flavocytochrome, nmr, paramagnetic shiftsfumarate reductase, cytochrome c(3), desulfovibrio-vulgaris, energytransduction, putrefaciens mr-1, electron-transfer, heme core, cooperativity, respiration, ncimb400
Subjects: Q Science
Q Science > QD Chemistry
ePrint ID: 20064
Date :
Date Event
3 December 2003Published
Date Deposited: 23 Feb 2006
Last Modified: 16 Apr 2017 23:00
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/20064

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