Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Richardson, David J.

doi:10.1099/00221287-146-3-551

Cited by 485 publications

(319 citation statements)

References 140 publications

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“…28 When the NapABC system is present, during aerobic respiration where O 2 is the terminal electron acceptor, so are two additional routes for QH 2 oxidation, namely, a cytochrome bo 3 quinol-oxidase and the cytochrome bc 1 -complex that delivers electrons to cytochrome aa 3 -and cbb 3 -type oxidases via cytochrome c, Fig. 4.…”

Section: Electrochemical Potential As a Determinant Of Electron Flux mentioning

confidence: 99%

The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry

Gates

Kemp

et al. 2011

Phys. Chem. Chem. Phys.

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In protein film electrochemistry a redox protein of interest is studied as an electroactive film adsorbed on an electrode surface. For redox enzymes this configuration allows quantification of the relationship between catalytic activity and electrochemical potential. Considered as a function of enzyme environment, i.e., pH, substrate concentration etc., the activity-potential relationship provides a fingerprint of activity unique to a given enzyme. Here we consider the nature of the activity-potential relationship in terms of both its cellular impact and its origin in the structure and catalytic mechanism of the enzyme. We propose that the activity-potential relationship of a redox enzyme is tuned to facilitate cellular function and highlight opportunities to test this hypothesis through computational, structural, biochemical and cellular studies.

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Section: Electrochemical Potential As a Determinant Of Electron Flux mentioning

confidence: 99%

The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry

Gates

Kemp

et al. 2011

Phys. Chem. Chem. Phys.

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“…Formate oxidation might also be part of a mechanism to form a proton gradient, once small uncharged molecules such as formic acid can cross the cytoplasmic membrane to the periplasmic space and release two protons after oxidation [2,3]. Prokaryote Fdhs are metalloenzymes with different subunit composition containing either molybdenum or tungsten at the active site.…”

Section: Introductionmentioning

confidence: 99%

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

et al. 2011

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Metal-dependent formate dehydrogenases (Fdh) from prokaryotic organisms are members of the dimethyl sulfoxide reductase family of mononuclear molybdenum-containing and tungsten-containing enzymes. Fdhs catalyze the oxidation of the formate anion to carbon dioxide in a redox reaction that involves the transfer of two electrons from the substrate to the active site. The active site in the oxidized state comprises a hexacoordinated molybdenum or tungsten ion in a distorted trigonal prismatic geometry. Using this structural model, we calculated the catalytic mechanism of Fdh through density functional theory tools. The simulated mechanism was correlated with the experimental kinetic properties of three different Fdhs isolated from three different Desulfovibrio species. Our studies indicate that the C-H bond break is an event involved in the rate-limiting step of the catalytic cycle. The role in catalysis of conserved amino acid residues involved in metal coordination and near the metal active site is discussed on the basis of experimental and theoretical results.

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“…Nitrate reduction occurs in the cell in order to incorporate nitrogen into biomolecules (assimilatory ammonification) as the final electron acceptor when bacteria are grown in anaerobic conditions (denitrification) and to eliminate energy excess generated by the cell metabolism (dissimilatory ammonification) [1][2][3]. Nitrate reductases (NRs) are enzymes that catalyze the reduction of nitrate according to the reaction:…”

Section: Introductionmentioning

confidence: 99%

“…criteria, such as localization of the enzyme in the cell, molecular properties of the catalytic center, and source: (1) eukaryotic NRs (Euk-NRs), (2) assimilatory NRs (Nas), (3) respiratory NRs (Nar), and (4) periplasmic NRs (Nap) [5,6]. Nas, Nar, and Nap, which are only found in prokaryotic organisms, belong to the dimethyl sulfoxide reductase family, whereas Euk-NRs belong to the sulfite oxidase family of molybdo proteins [4].…”

Section: Introductionmentioning

confidence: 99%

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

et al. 2006

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Nitrate reductases are enzymes that catalyze the conversion of nitrate to nitrite. We report here electron paramagnetic resonance (EPR) studies in the periplasmic nitrate reductase isolated from the sulfatereducing bacteria Desulfovibrio desulfuricans ATCC 27774. This protein, belonging to the dimethyl sulfoxide reductase family of mononuclear Mo-containing enzymes, comprises a single 80-kDa subunit and contains a Mo bis(molybdopterin guanosine dinucleotide) cofactor and a [4Fe-4S] cluster. EPR-monitored redox titrations, carried out with and without nitrate in the potential range from 200 to À500 mV, and EPR studies of the enzyme, in both catalytic and inhibited conditions, reveal distinct types of Mo(V) EPR-active species, which indicates that the Mo site presents high coordination flexibility. These studies show that nitrate modulates the redox properties of the Mo active site, but not those of the [4Fe-4S] center. The possible structures and the role in catalysis of the distinct Mo(V) species detected by EPR are discussed.

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Bacterial respiration: a flexible process for a changing environment 1999 Fleming Lecture (Delivered at the 144th meeting of the Society for General Microbiology, 8 September 1999)

Cited by 485 publications

References 140 publications

The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry

The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry

The mechanism of formate oxidation by metal-dependent formate dehydrogenases

EPR and redox properties of periplasmic nitrate reductase from Desulfovibrio desulfuricans ATCC 27774

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