The subunit composition and function of mammalian cytochrome c oxidase

Kadenbach, Bernhard; Hüttemann, Maik

doi:10.1016/j.mito.2015.07.002

Cited by 190 publications

(140 citation statements)

References 198 publications

(211 reference statements)

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“…Furthermore, the data demonstrate that a higher activity does not necessarily imply a "better" preparation. This is particularly evident from earlier studies of mammalian CytcO, which showed that addition of DDM at high concentration results in loss of regulatory subunits concomitantly with an increase in activity [32]. Similar results were observed earlier after preparation of other native nanodiscs from S. cerevisiae [8], from E. coli [4,9] or from R. sphaeroides [18].…”

Section: Spectral Characteristics and Activitysupporting

confidence: 84%

Isolation of yeast complex IV in native lipid nanodiscs

Смирнова

Sjöstrand

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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We used the amphipathic styrene maleic acid (SMA) co-polymer to extract cytochrome c oxidase (CytcO) in its native lipid environment from S. cerevisiae mitochondria. Native nanodiscs containing one CytcO per disc were purified using affinity chromatography. The longest cross-sections of the native nanodiscs were 11 nm x 14 nm. Based on this size we estimated that each CytcO was surrounded by ~100 phospholipids. The native nanodiscs contained the same major phospholipids as those found in the mitochondrial inner membrane.Even though CytcO forms a supercomplex with cytochrome bc 1 in the mitochondrial membrane, cyt. bc 1 was not found in the native nanodiscs. Yet, the loosely-bound Respiratory

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Section: Spectral Characteristics and Activitysupporting

confidence: 84%

Isolation of yeast complex IV in native lipid nanodiscs

Смирнова

Sjöstrand

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…Using this approach we confirmed the presence of all 13 subunits and also identified an associated protein, VDAC (UniProt ID P68002), with moderate sequence coverage (61%). VDAC was previously reported as associated with CcO but is not considered a constituent of the core complex (3,22).…”

Section: Resultsmentioning

confidence: 99%

“…Subunit VIb has been proposed to increase the stability of dimeric CcO, as suggested by its position in the crystal structure (3). In addition to dimeric CcO, a mitochondrial supercomplex containing monomeric CcO has been detected (21).…”

mentioning

confidence: 99%

“…Cytochrome c oxidase (CcO) is the last enzyme of the electron transport chain and receives electrons from cytochrome c molecules to catalyze the reduction of oxygen to water (1). CcO in bovine heart contains 13 different subunits (2) with various associated proteins with lower binding affinities (3). The three largest subunits (I-III) are encoded by mitochondrial genes (4) and form the core of the enzyme (5); subunits I and II contain metal binding sites, whereas subunit III stabilizes these catalytic centers and harbors the O 2 transfer pathway (6).…”

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confidence: 99%

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Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding

Liko

Degiacomi

Mohammed

et al. 2016

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

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Bovine cytochrome c oxidase is an integral membrane protein complex comprising 13 protein subunits and associated lipids. Dimerization of the complex has been proposed; however, definitive evidence for the dimer is lacking. We used advanced mass spectrometry methods to investigate the oligomeric state of cytochrome c oxidase and the potential role of lipids and posttranslational modifications in its subunit interfaces. Mass spectrometry of the intact protein complex revealed that both the monomer and the dimer are stabilized by large lipid entities. We identified these lipid species from the purified protein complex, thus implying that they interact specifically with the enzyme. We further identified phosphorylation and acetylation sites of cytochrome c oxidase, located in the peripheral subunits and in the dimer interface, respectively. Comparing our phosphorylation and acetylation sites with those found in previous studies of bovine, mouse, rat, and human cytochrome c oxidase, we found that whereas some acetylation sites within the dimer interface are conserved, suggesting a role for regulation and stabilization of the dimer, phosphorylation sites were less conserved and more transient. Our results therefore provide insights into the locations and interactions of lipids with acetylated residues within the dimer interface of this enzyme, and thereby contribute to a better understanding of its structure in the natural membrane. Moreover dimeric cytochrome c oxidase, comprising 20 transmembrane, six extramembrane subunits, and associated lipids, represents the largest integral membrane protein complex that has been transferred via electrospray intact into the gas phase of a mass spectrometer, representing a significant technological advance.cytochrome c oxidase | mass spectrometry | lipids

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“…Proton translocation by CcO contributes to the proton-motive force that powers ATP synthesis. The number of CcO subunits varies among different organisms, from four in prokaryotes [1] to thirteen in mammalian mitochondrial CcO [2–4]. Regardless of the origin, the catalytic core of CcO is composed of three highly hydrophobic subunits.…”

Section: Introductionmentioning

confidence: 99%

Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure

et al. 2016

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Delipidation of detergent-solubilized cytochrome c oxidase isolated from Rhodobacter sphaeroides (Rbs-CcO) has no apparent structural and/or functional effect on the protein, however affects its resistance against thermal or chemical denaturation. Phospholipase A2 (PLA2) hydrolysis of phospholipids that are co-purified with the enzyme removes all but two tightly bound phosphatidylethanolamines. Replacement of the removed phospholipids with nonionic detergent decreases both thermal stability of the enzyme and its resilience against the effect of chemical denaturants such as urea. In contrast to nondelipidated Rbs-CcO, the enzymatic activity of PLA2-treated Rbs-CcO is substantially diminished after exposure to high (>4M) urea concentration at room temperature without an alteration of its secondary structure. Absorbance spectroscopy and sedimentation velocity experiments revealed a strong correlation between intact tertiary structure of heme regions and quaternary structure, respectively, and the enzymatic activity of the protein. We concluded that phospholipid environment of Rbs-CcO has the protective role for stability of its tertiary and quaternary structures.

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The subunit composition and function of mammalian cytochrome c oxidase

Cited by 190 publications

References 198 publications

Isolation of yeast complex IV in native lipid nanodiscs

Isolation of yeast complex IV in native lipid nanodiscs

Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding

Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure

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