scholarly journals Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations

2019 ◽  
Vol 20 (15) ◽  
pp. 3830 ◽  
Author(s):  
María-Eugenia Llases ◽  
Marcos N. Morgada ◽  
Alejandro J. Vila
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
State Of The Art ◽  
Aerobic Respiration ◽  
Copper Site ◽  
The Family ◽  
Copper Sites ◽  
Heme Copper Oxidases ◽  
Copper Oxidase ◽  
Enzymatic Complex

Copper is an essential cofactor for aerobic respiration, since it is required as a redox cofactor in Cytochrome c Oxidase (COX). This ancient and highly conserved enzymatic complex from the family of heme-copper oxidase possesses two copper sites: CuA and CuB. Biosynthesis of the oxidase is a complex, stepwise process that requires a high number of assembly factors. In this review, we summarize the state-of-the-art in the assembly of COX, with special emphasis in the assembly of copper sites. Assembly of the CuA site is better understood, being at the same time highly variable among organisms. We also discuss the current challenges that prevent the full comprehension of the mechanisms of assembly and the pending issues in the field.

scholarly journals S11.25 X-ray structure of carbon monoxide at copper site of the dinuclear site of cytochrome c oxidase

2008 ◽  
Vol 1777 ◽  
pp. S71
Author(s):  
Kazumasa Muramoto ◽  
Naoki Nakagawa ◽  
Maki Taniguchi ◽  
Katsumasa Kanda ◽  
Kyoko Shinzawa-Itoh ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
X Ray ◽  
Copper Site

scholarly journals Photo-dependent binding structures of CO and NO on the heme-copper site in bovine cytochrome c oxidase

2010 ◽  
Vol 1797 ◽  
pp. 97-98
Author(s):  
Kazumasa Muramoto ◽  
Kazuhiro Ohta ◽  
Kyoko Shinzawa-Itoh ◽  
Eiki Yamashita ◽  
Tomitake Tsukihara ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Copper Site

scholarly journals Structure of the copper sites in membrane-bound cytochrome c oxidase.

1987 ◽  
Vol 262 (7) ◽  
pp. 3160-3164
Author(s):  
L. Powers ◽  
B. Chance ◽  
Y.C. Ching ◽  
C.P. Lee
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Membrane Bound ◽  
Copper Sites

scholarly journals The genus Microniphargus (Crustacea, Amphipoda): evidence for three lineages distributed across northwestern Europe and transfer from Niphargidae to Pseudoniphargidae

2021 ◽  
Vol 151 ◽  
Author(s):  
Dieter Weber ◽  
Fabio Stoch ◽  
Lee R.F.D. Knight ◽  
Claire Chauveau ◽  
Jean-François Flot
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Phylogenetic Analyses ◽  
Ribosomal Gene ◽  
Phylogenetic Position ◽  
Mitochondrial Cytochrome ◽  
Monotypic Genus ◽  
Centre Of Origin ◽  
Phylogenetic Studies ◽  
The Family

Microniphargus leruthi Schellenberg, 1934 (Amphipoda: Niphargidae) was first described based on samples collected in Belgium and placed in a monotypic genus within the family Niphargidae. However, some details of its morphology as well as recent phylogenetic studies suggest that Microniphargus may be more closely related to Pseudoniphargus (Amphipoda: Pseudoniphargidae) than to Niphargus. Moreover, M. leruthi ranges over 1,469 km from Ireland to Germany, which is striking since only a few niphargids have confirmed ranges in excess of 200 km. To find out the phylogenetic position of M. leruthi and check whether it may be a complex of cryptic species, we collected material from Ireland, England and Belgium then sequenced fragments of the mitochondrial cytochrome c oxidase subunit 1 gene as well as of the nuclear 28S ribosomal gene. Phylogenetic analyses of both markers confirm that Microniphargus is closer to Pseudoniphargus than to Niphargus, leading us to reallocate Microniphargus to Pseudoniphargidae. We also identify three congruent mito-nuclear lineages present respectively in Ireland, in both Belgium and England, and in England only (with the latter found in sympatry at one location), suggesting that M. leruthi is a complex of at least three species with a putative centre of origin in England.

Cytochrome aa3 in facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense

2005 ◽  
Vol 51 (8) ◽  
pp. 621-627 ◽  
Author(s):  
Takuro Nunoura ◽  
Yoshihiko Sako ◽  
Takayoshi Wakagi ◽  
Aritsune Uchida
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Gene Product ◽  
Respiratory Chain ◽  
Oxidase Activity ◽  
Terminal Oxidase ◽  
Hyperthermophilic Archaeon ◽  
Consumption Activity ◽  
Copper Oxidase

We partially purified and characterized the cytochrome aa3 from the facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense. This cytochrome aa3 showed oxygen consumption activity with N, N, N′, N′-tetramethyl-1,4-phenylenediamine and ascorbate as substrates, and also displayed bovine cytochrome c oxidase activity. These enzymatic activities of cytochrome aa3 were inhibited by cyanide and azide. This cytochrome contained heme As, but not typical heme A. An analysis of trypsin-digested fragments indicated that 1 subunit of this cytochrome was identical to the gene product of subunit I of the SoxM-type heme – copper oxidase (poxC). This is the first report of a terminal oxidase in hyperthermophilic crenarchaeon belonging to the order Thermoproteales.Key words: aerobic respiratory chain, terminal oxidase, Archaea, hyperthermophile, Pyrobaculum.

scholarly journals Yeast cytochrome c oxidase: A model system to study mitochondrial forms of the haem–copper oxidase superfamily

2012 ◽  
Vol 1817 (4) ◽  
pp. 620-628 ◽  
Author(s):  
Amandine Maréchal ◽  
Brigitte Meunier ◽  
David Lee ◽  
Christine Orengo ◽  
Peter R. Rich
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Model System ◽  
Copper Oxidase

Biomimetic Systems for the “Visible” Copper-Site CuAin Cytochrome c Oxidase

1985 ◽  
Vol 25 (1) ◽  
pp. 56-65 ◽  
Author(s):  
Hans Toftlund ◽  
Jan Becher ◽  
Preben H. Olesen ◽  
Jens Z. Pedersen
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Biomimetic Systems ◽  
Copper Site
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