Structure at 1.3Å Resolution of Rhodothermus marinus caa3 Cytochrome c Domain

Srinivasan, Vasundara; Rajendran, Chitra; Sousa, Filipa L.; Melo, Ana M.; Saraiva, Lı́gia M.; Pereira, Manuela M.; Santana, Margarida; Teixeira, Miguel; Michel, Hartmut

doi:10.1016/j.jmb.2004.10.069

Cited by 18 publications

(20 citation statements)

References 38 publications

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“…The structure corroborates the modular character of ACIII and its role as a redox-driven proton pump. According to thermodynamics, the oxidoreduction reaction involves the electron transfer of two electrons from menaquinol, with a reduction potential of −70 mV, to an electron acceptor with a reduction potential of +250 mV, which provides enough energy for pumping up to four protons 4 , 11 , 38 . The mechanism proposed here identifies the possible players responsible for quinol oxidation, proton translocation, and subunit crosstalk, and thus paves the way for testable hypotheses on the energy transduction mechanism of this complex.…”

Section: Discussionmentioning

confidence: 99%

Structural basis for energy transduction by respiratory alternative complex III

et al. 2018

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Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron–sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.

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Section: Discussionmentioning

confidence: 99%

Structural basis for energy transduction by respiratory alternative complex III

et al. 2018

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“…However, this is most probably a methionine residue in the conserved motive MPA present in other cytochromes (e.g. [28]). No transmembrane helices were predicted to be present.…”

Section: Gene Cluster Organization and Gene Sequence Analysismentioning

confidence: 99%

The alternative complex III from Rhodothermus marinus – A prototype of a new family of quinol:electron acceptor oxidoreductases

Pereira¹,

Refojo²,

Hreggviðsson³

et al. 2007

FEBS Letters

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The biochemical and genetic search for a bc 1 complex in Rhodothermus marinus was always fruitless; however, a functional equivalent, i.e. having quinol:cytochrome c oxidoreductase activity was characterized. Now, with the sequencing of R. marinus genome, it was possible to assign the N-terminal sequences of several proteins of this complex to its coding genes. The alternative complex III from R. marinus has the same genomic organization of the so-called MFIcc complexes, proposed to be oxidoreductases of the respiratory and photosynthetic electron transfer chains. In this report, we establish undoubtedly the existence of an alternative complex III, a functional substitute of the bc 1 complex, by its identification at both the biochemical and genomic level.

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“…6a) on the basis of sequence homology. In particular, four models were created using the structures of the following c-type-heme-containing templates: Rhodothermus marinus caa 3 cytochrome c domain (1W2L [57]), C-terminal domain of quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5 (1KV9 [58]), the monohemic cytochrome c 2 from Rhodopila globiformis (1HRO [59]), and the monohemic cytochrome c from R. marinus (3CP5 [60]). The latter has the highest sequence identity (25%) and the model obtained gave the best results in the docking study.…”

Section: Electron Transfer Pathwaymentioning

confidence: 99%

The electron transfer complex between nitrous oxide reductase and its electron donors

Dell’Acqua

Moura

et al. 2011

J Biol Inorg Chem

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Identifying redox partners and the interaction surfaces is crucial for fully understanding electron flow in a respiratory chain. In this study, we focused on the interaction of nitrous oxide reductase (N 2 OR), which catalyzes the final step in bacterial denitrification, with its physiological electron donor, either a c-type cytochrome or a type 1 copper protein. The comparison between the interaction of N 2 OR from three different microorganisms, Pseudomonas nautica, Paracoccus denitrificans, and Achromobacter cycloclastes, with their physiological electron donors was performed through the analysis of the primary sequence alignment, electrostatic surface, and molecular docking simulations, using the bimolecular complex generation with global evaluation and ranking algorithm. The docking results were analyzed taking into account the experimental data, since the interaction is suggested to have either a hydrophobic nature, in the case of P. nautica N 2 OR, or an electrostatic nature, in the case of P. denitrificans N 2 OR and A. cycloclastes N 2 OR. A set of well-conserved residues on the N 2 OR surface were identified as being part of the electron transfer pathway from the redox partner to N 2 OR (Ala495, Asp519, Val524, His566 and Leu568 numbered according to the P. nautica N 2 OR sequence). Moreover, we built a model for Wolinella succinogenes N 2 OR, an enzyme that has an additional c-type-heme-containing domain. The structures of the N 2 OR domain and the c-type-heme-containing domain were modeled and the full-length structure was obtained by molecular docking simulation of these two domains. The orientation of the c-type-heme-containing domain relative to the N 2 OR domain is similar to that found in the other electron transfer complexes.

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Structure at 1.3Å Resolution of Rhodothermus marinus caa3 Cytochrome c Domain

Cited by 18 publications

References 38 publications

Structural basis for energy transduction by respiratory alternative complex III

Structural basis for energy transduction by respiratory alternative complex III

The alternative complex III from Rhodothermus marinus – A prototype of a new family of quinol:electron acceptor oxidoreductases

The electron transfer complex between nitrous oxide reductase and its electron donors

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