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Nicholas P. J. Cotton

Researcher at University of Birmingham

Publications -  12
Citations -  288

Nicholas P. J. Cotton is an academic researcher from University of Birmingham. The author has contributed to research in topics: Electron transport chain & Rhodobacter. The author has an hindex of 8, co-authored 12 publications receiving 283 citations.

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Journal ArticleDOI

The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase.

TL;DR: The asymmetry of the dI:dIII complex suggests that in the intact enzyme there is an alternation of conformation at the catalytic sites associated with changes in nucleotide binding during proton translocation.
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The effect of venturicidin on light and oxygen-dependent electron transport, proton translocation, membrane potential development and ATP synthesis in intact cells of Rhodopseudomonas capsulata

TL;DR: Venturicidin behaves as an orthodox energy transfer inhibitor in intact cells of Rhodopseudomonas capsulata as judged by the following criteria: it led to inhibition of respiration, and inhibited the rise in cellular ATP concentration accompanying either photosynthesis or respiration.
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Interaction between the Respiratory and Photosynthetic Electron Transport Chains of Intact Cells of Rhodopseudomonas capsulata Mediated by Membrane Potential

TL;DR: Evidence that light-inhibition of respiration is mediated by delta psi is interpreted as evidence that uncoupling agents affect the response by uncouplers, inhibitors and with light intensity.
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The coupling between protonmotive force and the NAD(P)+ transhydrogenase in chromatophores from photosynthetic bacteria.

TL;DR: Data from chromatophores in illuminated and darkened suspensions are used in an attempt to discriminate between two models of energy transduction: (a) the driving force exerted by the membrane potential is mediated by a pH gradient formed through the operation of a proton well in the transhydrogenase; (b) the membranes potential increases a rate constant for charge translocation through transHydrogenase by decreasing the effective height of the Eyring barrier for charge transfer across the membrane through the enzyme.