Menaquinone-7 Is Specific Cofactor in Tetraheme Quinol Dehydrogenase CymA

McMillan, Duncan G. G.; Marritt, Sophie J.; Butt, Julea N.; Jeuken, Lars J. C.

doi:10.1074/jbc.m112.348813

Cited by 94 publications

(100 citation statements)

References 66 publications

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“…For instance, in this journal Gao et al (2009) assumed that electron transfer between CymA and NapAB is direct and does not involve a further electron shuttling protein. Other researchers raised the hypothesis that CymA would form electron transfer complexes with the outer membrane anchored terminal reductases MtrABC or DmsABEF (Ross et al, 2011;McMillan et al, 2012). Nevertheless, this study reveals the necessity of at least one connecting protein, either FccA or STC for coupling respiratory oxidation of CymA to effective electron transfer to at least ferric citrate, DMSO and nitrate.…”

Section: Discussionmentioning

confidence: 63%

A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime

et al. 2015

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Microorganisms show an astonishing versatility in energy metabolism. They can use a variety of different catabolic electron acceptors, but they use them according to a thermodynamic hierarchy, which is determined by the redox potential of the available electron acceptors. This hierarchy is reflected by a regulatory machinery that leads to the production of respiratory chains in dependence of the availability of the corresponding electron acceptors. In this study, we showed that the c-proteobacterium Shewanella oneidensis produces several functional electron transfer chains simultaneously. Furthermore, these chains are interconnected, most likely with the aid of c-type cytochromes. The cytochrome pool of a single S. oneidensis cell consists of ca. 700 000 hemes, which are reduced in the absence on an electron acceptor, but can be reoxidized in the presence of a variety of electron acceptors, irrespective of prior growth conditions. The small tetraheme cytochrome (STC) and the soluble heme and flavin containing fumarate reductase FccA have overlapping activity and appear to be important for this electron transfer network. Double deletion mutants showed either delayed growth or no growth with ferric iron, nitrate, dimethyl sulfoxide or fumarate as electron acceptor. We propose that an electron transfer machinery that is produced irrespective of a thermodynamic hierarchy not only enables the organism to quickly release catabolic electrons to a variety of environmental electron acceptors, but also offers a fitness benefit in redox-stratified environments.

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Section: Discussionmentioning

confidence: 63%

A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime

et al. 2015

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“…In this study, the detected outer membrane cytochrome c genes included decaheme OmcA/MtrC (Richter et al, 2012a), MtrF (a homologue of OmcA/MtrC) (Coursolle and Gralnick, 2010), and OmpA. Periplasmic multi-heme cytochrome c including one decaheme MtrA, 11 decaheme DmsE (a homologue of MtrA) (Coursolle and Gralnick, 2010), 3 inner membrane anchored (periplasm side) tetraheme NapC/NirT (a homologue of quinol dehydrogenase CymA) (McMillan et al, 2012) and 2 transmembrane high-molecular-weight cytochrome electron-transferring complexes were detected (Fig. 7).…”

Section: C-type Cytochrome Genes Suggest Direct Electron Transfermentioning

confidence: 97%

“…At neutral pH, the RP window of MtrC/OmcA, MtrF, MtrA and CymA are À0.5 to 0.1 V, À0.4 to 0.1 V, À0.3 to 0 V and À0.4 to 0 V, respectively (Clarke et al, 2011;Firer-Sherwood et al, 2008;McMillan et al, 2012;Ross et al, 2011). Supply of the periplasmic electrons acceptor fumarate to a Shewanella oneidensis MR-1 formed biocathode (poised at À0.36 V) immediately led to electrons uptake for fumarate reduction, while a mutant lacking MtrA, MtrB or the menaquinone-linked CymA displayed a severe reduction deficiency, which showed that electrons primarily flowed from outer membrane cytochromes into the menaquinone pool, and then back to periplasmic fumarate reductase (Ross et al, 2011).…”

Section: C-type Cytochrome Genes Suggest Direct Electron Transfermentioning

confidence: 99%

Microbial community structure and function of Nitrobenzene reduction biocathode in response to carbon source switchover

et al. 2014

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“…Protein film electrochemistry of multi-haem cytochromes from S. oneidensis. Cyclic voltammetry of CymA (solid line) adsorbed on an 8-mercaptoctanol modified template stripped gold electrode at a 10 mV s 21 scan rate, pH 7.4 is compared to a voltammogram recorded in the absence of CymA (broken line) (redrawn from [34]). Baseline-subtracted cyclic voltammograms are presented for MtrCAB, MtrA, MtrC and MtrF adsorbed on graphite electrodes.…”

Section: Redox Potentialsmentioning

confidence: 99%

Multi-haem cytochromes inShewanella oneidensisMR-1: structures, functions and opportunities

Breuer

Rosso

Blumberger

et al. 2015

J. R. Soc. Interface.

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219

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Multi-haem cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometres. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates, including electrodes and insoluble mineral oxides of Fe(III) and Mn(III/IV), by species of Shewanella and Geobacter. However, multihaem cytochromes are found in numerous and phylogenetically diverse prokaryotes where they participate in electron transfer and redox catalysis that contributes to biogeochemical cycling of N, S and Fe on the global scale. These properties of multi-haem cytochromes have attracted much interest and contributed to advances in bioenergy applications and bioremediation of contaminated soils. Looking forward, there are opportunities to engage multi-haem cytochromes for biological photovoltaic cells, microbial electrosynthesis and developing bespoke molecular devices. As a consequence, it is timely to review our present understanding of these proteins and we do this here with a focus on the multitude of functionally diverse multi-haem cytochromes in Shewanella oneidensis MR-1. We draw on findings from experimental and computational approaches which ideally complement each other in the study of these systems: computational methods can interpret experimentally determined properties in terms of molecular structure to cast light on the relation between structure and function. We show how this synergy has contributed to our understanding of multi-haem cytochromes and can be expected to continue to do so for greater insight into natural processes and their informed exploitation in biotechnologies.

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Menaquinone-7 Is Specific Cofactor in Tetraheme Quinol Dehydrogenase CymA

Cited by 94 publications

References 66 publications

A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime

A dynamic periplasmic electron transfer network enables respiratory flexibility beyond a thermodynamic regulatory regime

Microbial community structure and function of Nitrobenzene reduction biocathode in response to carbon source switchover

Multi-haem cytochromes inShewanella oneidensisMR-1: structures, functions and opportunities

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