Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from <i>Chlamydomonas reinhardtii</i>

Rumpel, Sigrun; Siebel, Judith F.; Diallo, Mamou; Farès, Christophe; Reijerse, Edward J.; Lubitz, Wolfgang

doi:10.1002/cbic.201500130

Cited by 34 publications

(14 citation statements)

References 43 publications

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“…Fd transfers electrons from PSI to several target enzymes through the formation of electron transfer protein complexes predominantly by electrostatic interactions. All residues implicated in the interactions of Fd with various enzymatic partners (Akashi et al ., ; García‐Sánchez et al ., ; Kurisu et al ., ; Hanke et al ., ; Maeda et al ., ; Saitoh et al ., ; Chang et al ., ; Winkler et al ., ; Sakakibara et al ., ; Rumpel et al ., ) were conserved in the psychrophile UWO241 (Fig. ).…”

Section: Resultsmentioning

confidence: 97%

Characterization of photosynthetic ferredoxin from the Antarctic alga Chlamydomonas sp. UWO241 reveals novel features of cold adaptation

et al. 2018

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The objective of this work was to characterize photosynthetic ferredoxin from the Antarctic green alga Chlamydomonas sp. UWO241, a key enzyme involved in distributing photosynthetic reducing power. We hypothesize that ferredoxin possesses characteristics typical of cold-adapted enzymes, namely increased structural flexibility and high activity at low temperatures, accompanied by low stability at moderate temperatures. To address this objective, we purified ferredoxin from UWO241 and characterized the temperature dependence of its enzymatic activity and protein conformation. The UWO241 ferredoxin protein, RNA, and DNA sequences were compared with homologous sequences from related organisms. We provide evidence for the duplication of the main ferredoxin gene in the UWO241 nuclear genome and the presence of two highly similar proteins. Ferredoxin from UWO241 has both high activity at low temperatures and high stability at moderate temperatures, representing a novel class of cold-adapted enzymes. Our study reveals novel insights into how photosynthesis functions in the cold. The presence of two distinct ferredoxin proteins in UWO241 could provide an adaptive advantage for survival at cold temperatures. The primary amino acid sequence of ferredoxin is highly conserved among photosynthetic species, and we suggest that subtle differences in sequence can lead to significant changes in activity at low temperatures.

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Section: Resultsmentioning

confidence: 97%

Characterization of photosynthetic ferredoxin from the Antarctic alga Chlamydomonas sp. UWO241 reveals novel features of cold adaptation

et al. 2018

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“…In biology, the buried H cluster in CrHydA1 must exchange electrons directly with a small protein-a ferredoxin known as PetF-in encounters that are necessarily transient but likely to be more efficient in regard to electronic coupling than achieved with an electrode. A calculated protein-protein structure suggests a distance of 11 Å between the H cluster of CrHydA1 and the [2Fe-2S] cluster of PetF (32). Negligible differences between the blank and CO-inhibited enzymes, in the values of all of the elements, reflect the fact that the inhibitor CO acts as an excellent "off" switch in both cases (24): notably, noncatalytic electron transfers to and within the enzyme barely register in the EIS experiments.…”

Section: Electrochemical Impedance Spectroscopymentioning

confidence: 96%

Frequency and potential dependence of reversible electrocatalytic hydrogen interconversion by [FeFe]-hydrogenases

Pandey

Islam

Happe

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The kinetics of hydrogen oxidation and evolution by [FeFe]hydrogenases have been investigated by electrochemical impedance spectroscopy-resolving factors that determine the exceptional activity of these enzymes, and introducing an unusual and powerful way of analyzing their catalytic electron transport properties. Attached to an electrode, hydrogenases display reversible electrocatalytic behavior close to the 2H + /H 2 potential, making them paradigms for efficiency: the electrocatalytic "exchange" rate (measured around zero driving force) is therefore an unusual parameter with theoretical and practical significance. Experiments were carried out on two [FeFe]-hydrogenases, CrHydA1 from the green alga Chlamydomonas reinhardtii, which contains only the active-site "H cluster," and CpI from the fermentative anaerobe Clostridium pasteurianum, which contains four low-potential FeS clusters that serve as an electron relay in addition to the H cluster. Data analysis yields catalytic exchange rates (at the formal 2H + /H 2 potential, at 0°C) of 157 electrons (78 molecules H 2 ) per second for CpI and 25 electrons (12 molecules H 2 ) per second for CrHydA1. The experiments show how the potential dependence of catalytic electron flow comprises frequency-dependent and frequency-independent terms that reflect the proficiencies of the catalytic site and the electron transfer pathway in each enzyme. The results highlight the "wire-like" behavior of the Fe-S electron relay in CpI and a low reorganization energy for electron transfer on/off the H cluster.hydrogen | electrocatalysis | impedance spectroscopy | hydrogenase | electron transfer

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“…In addition, the development of artificial in vitro maturation systems for hydrogenases in a great variety of different scaffolds could help to improve our fundamental understanding of hydrogenases, including the potential limiting factors, spectroscopic studies of the active center and the effects of O 2 on the enzyme activity. The successful in vitro maturation system can provide catalytically active hydrogenase subunits used for protein-protein docking studies with enzymes demanding low-potential electrons such as formate dehydrogenase or CO dehydrogenase [127,201]. Indeed, this strategy facilitates their potential application in industrially useful H 2 -conversion catalysts.…”

Section: Discussionmentioning

confidence: 99%

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Fan

Neubauer

Lenz

et al. 2020

IJMS

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Hydrogenases are complex metalloenzymes, showing tremendous potential as H2-converting redox catalysts for application in light-driven H2 production, enzymatic fuel cells and H2-driven cofactor regeneration. They catalyze the reversible oxidation of hydrogen into protons and electrons. The apo-enzymes are not active unless they are modified by a complicated post-translational maturation process that is responsible for the assembly and incorporation of the complex metal center. The catalytic center is usually easily inactivated by oxidation, and the separation and purification of the active protein is challenging. The understanding of the catalytic mechanisms progresses slowly, since the purification of the enzymes from their native hosts is often difficult, and in some case impossible. Over the past decades, only a limited number of studies report the homologous or heterologous production of high yields of hydrogenase. In this review, we emphasize recent discoveries that have greatly improved our understanding of microbial hydrogenases. We compare various heterologous hydrogenase production systems as well as in vitro hydrogenase maturation systems and discuss their perspectives for enhanced biohydrogen production. Additionally, activities of hydrogenases isolated from either recombinant organisms or in vivo/in vitro maturation approaches were systematically compared, and future perspectives for this research area are discussed.

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Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii

Cited by 34 publications

References 43 publications

Characterization of photosynthetic ferredoxin from the Antarctic alga Chlamydomonas sp. UWO241 reveals novel features of cold adaptation

Characterization of photosynthetic ferredoxin from the Antarctic alga Chlamydomonas sp. UWO241 reveals novel features of cold adaptation

Frequency and potential dependence of reversible electrocatalytic hydrogen interconversion by [FeFe]-hydrogenases

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

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