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John R. Guest

Researcher at University of Sheffield

Publications -  216
Citations -  13822

John R. Guest is an academic researcher from University of Sheffield. The author has contributed to research in topics: Escherichia coli & Gene. The author has an hindex of 73, co-authored 216 publications receiving 13499 citations. Previous affiliations of John R. Guest include Ontario Institute for Cancer Research.

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FNR and its role in oxygen-regulated gene expression in Escherichia coli

TL;DR: It is clear that oxygen functions as a regulatory signal controlling several important aspects of mitcrobial physiology, and further studies should reveal the molecular basis of the mechanism by which changes in oxygen tension are sensed.
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FNR and its role in oxygen-regulated gene expression in

TL;DR: The purpose of this review is to summarize what is known about FNR, the transcriptional regulator which is essential for expressing anaerobic respiratory processes in E. coli.
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A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.

TL;DR: It is proposed that Hyf, in conjunction with formate dehydrogenase H (Fdh-H), forms a hitherto unrecognized respiration-linked proton-translocating formate hydrogenlyase (FHL-2) that is likely to act as a formate-dependent regulator of the hyf operon and that FocB provides the Hyf complex with external formate as substrate.
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Ferritin Mutants of Escherichia coli Are Iron Deficient and Growth Impaired, and fur Mutants are Iron Deficient

TL;DR: It is concluded that FtnA acts as an iron store accommodating up to 50% of the cellular iron during postexponential growth in iron-rich media and providing a source of iron that partially compensates for iron deficiency during iron-restricted growth.
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Two biochemically distinct classes of fumarase in Escherichia coli

TL;DR: Biochemical studies with strains of Escherichia coli that are amplified for the products of the three fumarase genes have shown that there are two distinct classes of fumarases, and it is suggested that the Class I enzymes may belong to a wider family of iron-dependent carboxylic acid hydro-lyases that includes maleate dehydratase and aconitase.