Unveiling the Details of Electron Transfer in Multicenter Redox Proteins

Paquete, Catarina M.; Louro, Ricardo O.

doi:10.1021/ar4000696

Cited by 58 publications

(48 citation statements)

References 50 publications

(94 reference statements)

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“…The affinities reported in [84] fell into the mM range (similar to the cytochrome -cytochrome interactions from §4.2.1), suggesting only transient interactions as would be consistent with the role as an electron shuttle. While a role for flavins as electron shuttle has also been established experimentally [49,142], their exact role or portfolio of roles is still a matter of debate: a recent study [51] suggests the OM cytochromes MtrC and OmcA in fact stably bind flavin molecules as cofactors which then interact with solid substrates.…”

Section: Soluble Substratessupporting

confidence: 52%

“…The experimental determination of microscopic redox potentials requires a means of distinguishing the different redox centres. Nuclear magnetic resonance (NMR) spectroscopy can be employed for this purpose as the (highly redox-sensitive) signals for methyl groups of different haems can be distinguished in spite of the overall nearly identical chemical nature of bis-His-ligated c-haems [84,85]. At the same time, electrostatic interactions between haems can be established, quantifying how the redox potential of one haem is shifted by a different redox state of another haem.…”

Section: Redox Potentialsmentioning

confidence: 99%

“…In [84], the interaction of several OM cytochromes of S. oneidensis with several redox shuttles was thus investigated, yielding only in some cases interactions close to a haem. However, even in these cases the interaction could not be localized to a specific cofactor or set of cofactors.…”

Section: Soluble Substratesmentioning

confidence: 99%

“…For the case of docking to multi-haem cytochromes as in [84], the problem is of course that it is not even known which one(s) of the many solventexposed haem cofactors might be potential binding site(s) for a given substrate to begin with. Therefore, such docking studies need to be done in a 'blind' manner, searching all relevant regions of the cytochrome (e.g.…”

Section: Soluble Substratesmentioning

confidence: 99%

See 3 more Smart Citations

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

Breuer

Rosso

Blumberger

et al. 2015

J. R. Soc. Interface.

206

182

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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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Section: Soluble Substratessupporting

confidence: 52%

Section: Redox Potentialsmentioning

confidence: 99%

Section: Soluble Substratesmentioning

confidence: 99%

Section: Soluble Substratesmentioning

confidence: 99%

See 2 more Smart Citations

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

Breuer

Rosso

Blumberger

et al. 2015

J. R. Soc. Interface.

206

182

View full text Add to dashboard Cite

show abstract

“…Furthermore, we posit that the frequent transient encounters among these crowded proteins favor protein conformations that create the concerted kinetic behavior and the single functional macroscopic reduction potential of 650 mV observed in situ. We speculate that the in situ electron transfer behavior described herein may be the rule, rather than the exception, in those chemolithotrophic bacteria that respire either aerobically or anaerobically with extracellular substrates (47)(48)(49). We note that transient interactions among multiheme cytochromes are widespread in the periplasmic spaces of Shewanella species that pass electrons to extracellular, insoluble iron oxides (50 -53).…”

Section: Discussionmentioning

confidence: 85%

The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant

Painter

Ban

et al. 2015

Journal of Biological Chemistry

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Background:The order of electron transfer in the respiratory chain of Acidithiobacillus ferrooxidans is unknown. Results:The multicenter respiratory chain functioned as an ensemble with a single macroscopic rate constant. Conclusion:The crowded respiratory proteins behaved as would a single protein with a common standard reduction potential of 650 mV. Significance: In situ spectroscopy constitutes a new and effective means to study cellular respiration.

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Respiration in Electroactive Bacteria: Bioinorganic Aspects

Behan,

Louro,

Barrière

2023

Encyclopedia of Inorganic and Bioinorganic Chemistry

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This article gives an up‐to‐date (2023) account on the bioinorganic basis for extracellular electron transfer (EET) in electroactive bacteria. These microorganisms connect their respiratory metabolism to extracellular solid electron acceptors or donors, typically metal oxides of iron or manganese. Thanks to this peculiar property, electroactive bacteria can develop as biofilms at electrodes, be studied electrochemically, and form the basis of diverse potential applications termed microbial electrochemical systems (MES). The metalloproteins forming the respiratory chain from NADH oxidation to the reduction of the terminal solid electron acceptor are described in detail for the most studied Gram‐negative electroactive strains developed at anodes: Shewanella oneidensis MR‐1 and Geobacter sulfurreducens . Although less efficient than their Gram‐negative counterpart and sometimes referred to as weak electricigens, an example of electroactive anodophile Gram‐positive bacteria, Thermincola sp., is also discussed. The key cytochromes involved in the electron transport chain are discussed such as outer membrane c ‐type cytochromes (Omc) and multiheme cytochromes, forming by self‐assembly up to micrometer‐long electron conductive extracellular pili or nanowires. The case of microorganisms that uptake electrons from solid extracellular electron donors is addressed with a highlight on photoferrotrophs and cathodic denitrifying bacteria. Finally, the common strategy developed by different bacteria to electrically connect different types of respiratory metabolism is stressed together with the apparent ubiquity of EET across life domains including archaea.

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Unveiling the Details of Electron Transfer in Multicenter Redox Proteins

Cited by 58 publications

References 50 publications

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

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

The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant

Respiration in Electroactive Bacteria: Bioinorganic Aspects

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