Multi-heme proteins: Nature's electronic multi-purpose tool

Bewley, Kathryn D.; Ellis, Katie E.; Firer-Sherwood, Mackenzie A.; Elliott, Sean J.

doi:10.1016/j.bbabio.2013.03.010

Cited by 91 publications

(66 citation statements)

References 123 publications

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“…The encoded decaheme cytochrome c, DhcA, is most likely associated with the RnfG on the periplasmic side of the complex and could provide an electron conduit to the periplasmic cytochrome c pool in D. alaskensis str. G20 similar to the decaheme cytochrome c MtrA in Shewanella (Bewley et al ., ; Fonseca et al ., ). For strain G20, we propose that the DhcA‐Rnf complex couples the oxidation of reduced ferredoxin (RnfB) either with NAD + reduction in the cytoplasm (RnfC) or H + /CO 2 reduction in the periplasm (via DhcA – TpI‐c 3 – hydrogenases/formate dehydrogenases).…”

Section: Discussionmentioning

confidence: 99%

The energy‐conserving electron transfer system used by Desulfovibrio alaskensis strain G20 during pyruvate fermentation involves reduction of endogenously formed fumarate and cytoplasmic and membrane‐bound complexes, Hdr‐Flox and Rnf

Meyer

Kuehl

Price

et al. 2014

Environmental Microbiology

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The adaptation capability of Desulfovibrio to natural fluctuations in electron acceptor availability was evaluated by studying Desulfovibrio alaskensis strain G20 under varying respiratory, fermentative and methanogenic coculture conditions in chemostats. Transition from lactate to pyruvate in coculture resulted in a dramatic shift in the population structure and closer interspecies cell-to-cell interactions. Lower methane production rates in coculture than predicted from pyruvate input was attributed to redirection of electron flow to fumarate reduction. Without a methanogenic partner, accumulation of H₂and formate resulted in greater succinate production. Comparative transcript and gene fitness analysis in concert with physiological data of G20 wildtype and mutants demonstrated that pyruvate fermentation involves respiration of cytoplasmically formed fumarate using cytoplasmic and membrane-bound energy-conserving complexes, Rnf, Hdr-Flox-1 and Hmc. At the low H₂/formate levels maintained in coculture, Rnf likely functions as proton-pumping ferredoxin (Fd): type-I cytochrome c oxidoreductase, which transitions to a proton-pumping Fd(red): nicotinamide adenine dinucleotide (NAD⁺) oxidoreductase at high H₂/formate levels during fermentation in monoculture. Hdr-Flox-1 is postulated to recycle Fd(red) via a flavin-based electron bifurcation involving NADH, Fdox and the thiol/disulphide-containing DsrC. In a menaquinone (MQ)-based electron confurcation reaction, the high-molecular-weight cytochrome-c₃complex, Hmc, is proposed to then couple DsrC(red) and periplasmic H₂/formate oxidation using the MQ pool to fuel a membrane-bound fumarate reductase.

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Section: Discussionmentioning

confidence: 99%

The energy‐conserving electron transfer system used by Desulfovibrio alaskensis strain G20 during pyruvate fermentation involves reduction of endogenously formed fumarate and cytoplasmic and membrane‐bound complexes, Hdr‐Flox and Rnf

Meyer

Kuehl

Price

et al. 2014

Environmental Microbiology

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Section: Figurementioning

confidence: 99%

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Hosseinzadeh¹,

Lu²

2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

162

121

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Redox potentials are the major contributors to controlling the ET rates and thus regulating ET processes in the bioenergetics. To maximize the efficiency of the ET process, one needs to master the art of tuning of the E°, especially metalloproteins, as they represent major classes of ET proteins. In this review, we first describe the importance of tuning E° of ET centers, including the metalloproteins described above, and its role in regulating the ET in bioenergetic processes including photosynthesis and respiration. The major focus of this review is to summarize recent work in designing the ET centers, namely cupredoxins, cytochromes, and iron-sulfur proteins, and examples in design of protein networks involved these ET centers. We then discuss the factors that affect redox potentials of these ET centers including metal ion, the ligands to metal center and interactions beyond the primary ligand, especially non-covalent secondary coordination sphere interactions. We gave examples of strategies to fine-tune the redox potential using both natural and unnatural amino acids and native and nonnative cofactors. Several case studies are used to illustrate recent successes in this area. Outlooks for future endeavors are also provided.

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“…The heme synthesis pathway is active in all cell types, and heme is the precursor of other molecules besides haemoglobin . Although the last three enzymes are all active in the mitochondrion (Fig.…”

Section: Increased Levels Of Chromophoresmentioning

confidence: 99%

Evidence and conjecture about mechanisms of cutaneous disease in photodermatology

Porter

Anstey

2014

Experimental Dermatology

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Photosensitivity disorders are caused by a variety of mechanisms. Three common themes are as follows: excess chromophore allowing visible light energy to cause photodynamic damage, reduced DNA repair capacity to UV-induced DNA damage, and enhanced sensitivity to light-induced allergens mediated immunologically. Although the cause of each condition may be known, the precise pathogenesis underlying the photosensitivity has taken longer to understand. By focussing on three clinical disorders under each of these themes, we have explored the following: why erythropoietic protoporphyria differs so markedly from the other cutaneous porphyrias; how a DNA repair defect was eventually revealed to be the underlying cause of the vitamin B3 deficiency disorder of pellagra; an immunological explanation for the over reactivity to photoallergens in chronic actinic dermatitis.

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Multi-heme proteins: Nature's electronic multi-purpose tool

Cited by 91 publications

References 123 publications

The energy‐conserving electron transfer system used by Desulfovibrio alaskensis strain G20 during pyruvate fermentation involves reduction of endogenously formed fumarate and cytoplasmic and membrane‐bound complexes, Hdr‐Flox and Rnf

The energy‐conserving electron transfer system used by Desulfovibrio alaskensis strain G20 during pyruvate fermentation involves reduction of endogenously formed fumarate and cytoplasmic and membrane‐bound complexes, Hdr‐Flox and Rnf

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Evidence and conjecture about mechanisms of cutaneous disease in photodermatology

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