Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Stephen K Chapman"'
Autor:
Anne K. Jones, Christopher G. Mowat, Katherine L Pankhurst, Malcolm D. Walkinshaw, Stephen K Chapman, Caroline S Miles, Fraser A. Armstrong, Emma L Rothery, Graeme A Reid, Janette M. Hudson
Publikováno v:
Journal of Biological Chemistry. 281:20589-20597
The mechanism for fumarate reduction by the soluble fumarate reductase from Shewanella frigidimarina involves hydride transfer from FAD and proton transfer from the active-site acid, Arg-402. It has been proposed that Arg-402 forms part of a proton t
Publikováno v:
Biochemical Society Transactions. 30:658-662
Shewanella spp. demonstrate great variability in the use of terminal electron acceptors in anaerobic respiration; these include nitrate, fumarate, DMSO, trimethylamine oxide, sulphur compounds and metal oxides. These pathways open up possible applica
Autor:
Mary K. Doherty, R Moysey, David Leys, Christopher G. Mowat, Stephen K Chapman, Caroline S Miles, Paul Taylor, Graeme A Reid, Malcolm D. Walkinshaw
Publikováno v:
Biochemistry. 40:12292-12298
There is now overwhelming evidence supporting a common mechanism for fumarate reduction in the respiratory fumarate reductases. The X-ray structures of substrate-bound forms of these enzymes indicate that the substrate is well positioned to accept a
Autor:
Mary K. Doherty, R Moysey, Stephen K Chapman, Caroline S Miles, Emma L Rothery, Katherine L Pankhurst, Graeme A Reid
Publikováno v:
Journal of Inorganic Biochemistry. 86:361-370
Autor:
Graeme A Reid, Paul Taylor, Sara L. Pealing, Stephen K Chapman, Mary K. Doherty, R Moysey, Caroline S Miles, Malcolm D. Walkinshaw
Publikováno v:
Biochemistry. 39:10695-10701
The active sites of respiratory fumarate reductases are highly conserved, indicating a common mechanism of action involving hydride and proton transfer. Evidence from the X-ray structures of substrate-bound fumarate reductases, including that for the
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459(2-3):310-315
In the absence of oxygen many bacteria are able to utilise fumarate as a terminal oxidant for respiration. In most known organisms the fumarate reductases are membrane-bound iron-sulfur flavoproteins but Shewanella species produce a soluble, periplas
Publikováno v:
Nature Structural Biology. 6:1108-1112
The 1.8 A resolution crystal structure of the tetraheme flavocytochrome c3, Fcc3, provides the first mechanistic insight into respiratory fumarate reductases or succinate dehydrogenases. The multi-redox center, three-domain protein shows a 40 A long
Autor:
Karen L. Turner, Stephen K Chapman, H A Heering, Mary K. Doherty, Graeme A Reid, Fraser A. Armstrong
Publikováno v:
Biochemistry. 38:3302-3309
The thermodynamic and catalytic properties of flavocytochrome c3 from Shewanella frigidimarina have been studied using a combination of protein film voltammetry and solution methods. As measured by solution kinetics, maximum catalytic efficiencies fo
Autor:
António V. Xavier, Katherine L Pankhurst, Emma L Rothery, Miguel Pessanha, Stephen K Chapman, Carlos A. Salgueiro, David L. Turner, Graeme A Reid
Publikováno v:
Inorganica Chimica Acta. 356:379-381
Flavocytochrome c3 is a periplasmic fumarate reductase with Mr 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,