Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase

Wang, Kefei; Zhen, Yuejun; Sadoski, Robert C.; Grinnell, Susan; Geren, Lois; Ferguson‐Miller, Shelagh; Durham, Bill; Millett, Francis

doi:10.1074/jbc.274.53.38042

Cited by 78 publications

(86 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Electrons enter CcO from cytochrome c at the Cu A center, apparently via the indole ring of a tryptophan residue, W143 II (34)(35)(36). W143 II and Q142 II are highly conserved and at the center of the predicted interface between cytochrome c and CcO (37).…”

Section: Cis-peptide Bond Between Q142ii and W143ii At The Electron Tmentioning

confidence: 99%

Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase

Qin

Hiser

Mulichak

et al. 2006

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

Self Cite

284

385

View full text Add to dashboard Cite

Well ordered reproducible crystals of cytochrome c oxidase (CcO) from Rhodobacter sphaeroides yield a previously unreported structure at 2.0 Å resolution that contains the two catalytic subunits and a number of alkyl chains of lipids and detergents. Comparison with crystal structures of other bacterial and mammalian CcOs reveals that the positions occupied by native membrane lipids and detergent substitutes are highly conserved, along with amino acid residues in their vicinity, suggesting a more prevalent and specific role of lipid in membrane protein structure than often envisioned. Well defined detergent head groups (maltose) are found associated with aromatic residues in a manner similar to phospholipid head groups, likely contributing to the success of alkyl glycoside detergents in supporting membrane protein activity and crystallizability. Other significant features of this structure include the following: finding of a previously unreported crystal contact mediated by cadmium and an engineered histidine tag; documentation of the unique His-Tyr covalent linkage close to the active site; remarkable conservation of a chain of waters in one proton pathway (D-path); and discovery of an inhibitory cadmium-binding site at the entrance to another proton path (K-path). These observations provide important insight into CcO structure and mechanism, as well as the significance of bound lipid in membrane proteins.cadmium binding ͉ membrane protein structure ͉ proton-conducting water chains C ytochrome c oxidase (CcO) is the terminal enzyme in the electron transfer chain in eukaryotes and many bacteria. It provides the final electron sink by accepting electrons from cytochrome c and reducing oxygen to water (1). The energy generated from this reaction is used to translocate protons across the membrane against the membrane potential and pH gradient (2). The proton gradient so formed is then used to make ATP, a universal energy source. CcO is an intrinsic membrane protein with varying numbers of subunits from 3 in some bacteria to 13 in mammalian mitochondria. However, only subunits I and II, which contain the redox active heme and metal centers and are highly conserved among different species, are required for electron transfer and proton pumping activities. Other subunits, particularly the highly conserved subunit III, likely play key roles in stabilizing and regulating the enzyme activity and energy metabolism in general.Over the past decade, several x-ray crystal structures of aa 3 -type CcOs from bovine heart mitochondria and bacteria have been determined (3-8). However, the mechanism of vectorial translocation of protons by CcO remains to be solved (9). It is now recognized that water molecules play a critical role in facilitating and controlling proton transfer (10). Thus, highresolution crystal structures of different redox states and key mutants with defined waters are necessary to elucidate the energy conservation process. However, achieving a reproducible high-resolution structure of membrane proteins remains a ...

show abstract

Section: Cis-peptide Bond Between Q142ii and W143ii At The Electron Tmentioning

confidence: 99%

Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase

Qin

Hiser

Mulichak

et al. 2006

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

Self Cite

284

385

View full text Add to dashboard Cite

show abstract

“…Modeling suggests that cyt c binds to the enzyme at an acidic patch on subunit II (86,87). The cyt c heme is very near the Trp-104 (subunit II) indole ring, a residue that appears from mutagenesis experiments to be critical for rapid cyt c 3 Cu A ET (88)(89)(90)(91). Solomon and coworkers (92) Based on a tunneling currents analysis, Stuchebrukhov and colleagues (96) suggested a slightly different Cu A -to-cyt a coupling route through His-204.…”

Section: Protein-protein Reactionsmentioning

confidence: 99%

Long-range electron transfer

Gray

Winkler

2005

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

761

841

View full text Add to dashboard Cite

Recent investigations have shed much light on the nuclear and electronic factors that control the rates of long-range electron tunneling through molecules in aqueous and organic glasses as well as through bonds in donor-bridge-acceptor complexes. Couplings through covalent and hydrogen bonds are much stronger than those across van der Waals gaps, and these differences in coupling between bonded and nonbonded atoms account for the dependence of tunneling rates on the structure of the media between redox sites in Ru-modified proteins and protein-protein complexes.electron tunneling ͉ hopping ͉ glass ͉ protein

show abstract

“…Subunit II has two transmembrane helices that anchor a solvent-exposed domain, which provides the inner sphere ligands for the dinuclear Cu A center. Although there is no direct structural information on a cytochrome ccytochrome c oxidase complex, kinetic (4,5), mutagenic (6,7), and modeling (8) studies indicate that cytochrome c binds at a site near the Cu A center to allow for efficient electron transfer from cytochrome c to Cu A . Thus, electrons enter cytochrome c oxidase via Cu A and are transferred to the cytochrome a 3 -Cu B center through cytochrome a (9).…”

mentioning

confidence: 99%

Characterization of YpmQ, an Accessory Protein Required for the Expression of Cytochrome c Oxidase in Bacillus subtilis

Mattatall

Jazairi

Hill

2000

Journal of Biological Chemistry

108

View full text Add to dashboard Cite

A search of the Bacillus subtilis genome identifies a potential homolog, ypmQ, of the inner mitochondrial membrane protein Sco1 from yeast. Sco1 has been found to aid the delivery of copper to cytochrome c oxidase. B. subtilis expresses two members of the cytochrome oxidase family, a cytochrome c oxidase that has two copper centers, Cu A and Cu B , and a menaquinol oxidase that has only Cu B . Deletion of ypmQ in B. subtilis depresses expression of cytochrome c oxidase but not menaquinol oxidase. Levels of cytochrome c oxidase recover when copper is added to the growth medium of the ⌬ypmQ strain or when ypmQ is expressed from a plasmid. Neither treatment affects the amount or activity of menaquinol oxidase. YpmQ in which two conserved cysteines are replaced by serines and a conserved histidine is replaced by alanine do not complement the deletion of ypmQ even though these mutant forms are found in the membrane extract at a level similar to the wild type protein. We propose that the two cysteines and the histidine are critical for the function of YpmQ and suggest they are involved in copper exchange between YpmQ and the Cu A site of cytochrome c oxidase.

show abstract

Definition of the Interaction Domain for Cytochrome con Cytochrome c Oxidase

Abstract: The reaction between cytochrome c (Cc) and Rhodobacter sphaeroides cytochrome c oxidase (CcO) was studied using a cytochrome c derivative labeled with ruthenium trisbipyridine at lysine 55 (Ru-55-Cc).

Cited by 78 publications

References 60 publications

Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase

Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase

Long-range electron transfer

Characterization of YpmQ, an Accessory Protein Required for the Expression of Cytochrome c Oxidase in Bacillus subtilis

Contact Info

Product

Resources

About