A missing link between complex I and group 4 membrane-bound [NiFe] hydrogenases
Open accessAbstract
Complex I of respiratory chains is an energy transducing enzyme present in most bacteria, mitochondria and chloroplasts. It catalyzes the oxidation of NADH and the reduction of quinones, coupled to cation translocation across the membrane. The complex has a modular structure composed of several proteins most of which are identified in other complexes. Close relations between complex I and group 4 membrane-bound [NiFe] hydrogenases and some subunits of multiple resistance to pH (Mrp) Na(+)/H(+) antiporters have been observed before and the suggestion that complex I arose from the association of a soluble nicotinamide adenine dinucleotide (NAD(+)) reducing hydrogenase with a Mrp-like antiporter has been put forward. In this article we performed a thorough taxonomic profile of prokaryotic group 4 membrane-bound [NiFe] hydrogenases, complexes I and complex I-like enzymes. In addition we have investigated the different gene clustering organizations of such complexes. Our data show the presence of complexes related to hydrogenases but which do not contain the binding site of the catalytic centre. These complexes, named before as Ehr (energy-converting hydrogenases related complexes) are a missing link between complex I and group 4 membrane-bound [NiFe] hydrogenases. Based on our observations we put forward a different perspective for the relation between complex I and related complexes. In addition we discuss the evolutionary, functional and mechanistic implications of this new perspective. This article is part of a Special Issue entitled: The evolutionary aspects of bioenergetic systems.
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The predicted [NiFe]-hydrogenase of M. tuberculosis appears to be part of an Ehr complex.
“Upon closer inspection, the predicted [NiFe]-hydrogenase of M. tuberculosis appears to form part of an Ehr (Ech hydrogenase-related) complex (99, 100).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [100]
Section 4.1 identifies Ehr complexes as related to membrane-bound [NiFe] hydrogenases, and section 4.3 describes an Ehr type close to Ech. Neither passage identifies a predicted hydrogenase in M. tuberculosis or places it in an Ehr complex, so the organism-specific attribution is unsupported. (LLM, conf=0.79)
Experimental — accuracy not yet measuredThe interpretation that quinones, Q cycle, and cytochromes b and c arose later is supported by the remarkable homology of several subunits of complex I to FeFe trimeric hydrogenases, NiFe hydrogenases, ferredoxin-reducing subunits, Ech and Na+/H+ antiporters.
“This interpretation is supported by the remarkable homology of several subunits of complex I to the proteins discussed here: FeFe trimeric hydrogenases, NiFe hydrogenases, ferredoxin-reducing subunits, Ech and Na+/H+ antiporters [202].”
From Early bioenergetic evolution (2013) · cites this paper as [202]
Section 1.1 identifies complex I subunits homologous to membrane-bound [NiFe] hydrogenases, soluble NAD⁺-reducing hydrogenases, and Mrp Na⁺/H⁺ antiporters; Section 1.2 specifically maps several complex I subunits to Ech. Our copy does not establish the claimed homology to trimeric [FeFe] hydrogenases or ferredoxin-reducing subunits. The proposed later origin of quinones and cytochromes is the citing authors’ interpretation, not a finding attributed to this source by the citation. (LLM, conf=0.84)
Experimental — accuracy not yet measuredA Na+/H+ antiporter is a single protein and an ancient one that is a component of both Ech and Complex I.
“It is a single protein, and an ancient one that is also a component of both Ech and Complex I [202,203].”
From Early bioenergetic evolution (2013) · cites this paper as [202]
Section 4.4 (page unavailable) reports that a standalone Mrp-like protein has Na+/H+ antiporter activity, while section 4.2.1 describes an evolutionary relationship between antiporter-like subunits in hydrogenases and complex I. The paper does not establish that one ancient, single-protein Na+/H+ antiporter is itself a component of both Ech and Complex I; it discusses related subunits and presents parts of their evolutionary history as hypotheses. (LLM, conf=0.84)
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References 68 · Cited by 120
- Authors
- Marreiros, B. C., Batista, A. P., Duarte, A. M. S., & Pereira, M. M.
- Affiliations
- Universidade Nova de Lisboa (PT)
- Corresponding author
- Pereira, Manuela M.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2013-02
- Volume
- 1827
- Issue
- 2
- Pages
- 198-209
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2089351638
- Cited by
- 120
- References
- 68
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 8 · 2023: 3 · 2022: 6 · 2021: 7 · 2020: 10 · 2019: 13 · 2018: 10 · 2017: 5 · 2016: 18 · 2015: 9 · 2014: 10 · 2013: 11 · 2012: 1
- FWCI
- 3.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fundação para a Ciência e a Tecnologia (SFRH/BPD/80741/2011, SFRH/BPD/78075/2011, PTDC/QUI-BIQ/100302/2008, PEst-OE/EQB/LA0004/2011)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- complex I, NADH oxidation, quinone reduction, gene clustering, catalytic site
- MeSH terms
- Cell Membrane, Hydrogen-Ion Concentration, Hydrogenase, Oxidation-Reduction, Electron Transport Complex I
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