Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:cd01663    89 NNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMT 168

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:cd01663   169 LEKMPLFVWSVLITAFLLLLSLP 191

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMvenGAGTGWTVYPPLSAniahagasVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LdQTPLFVWAVGITALL*LLSLP 103
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFP 174

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:cd01663    89 NNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMT 168

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:cd01663   169 LEKMPLFVWSVLITAFLLLLSLP 191

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:MTH00116   98 NNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMS 177

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00116  178 QYQTPLFVWSVLITAVLLLLSLP 200

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:MTH00223   95 NNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQ 174

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00223  175 LERLPLFVWSVKVTAFLLLLSLP 197

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:MTH00183   98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAIS 177

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00183  178 QYQTPLFVWAVLITAVLLLLSLP 200

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:MTH00037   98 NNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMT 177

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00037  178 FDRLPLFVWSVFITAFLLLLSLP 200

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:MTH00182  100 NNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVT 179

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00182  180 FNRLPLFVWSILITAFLLLLSLP 202

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSaNIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:MTH00079   99 NNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00079  178 LEHMSLFVWTVFVTVFLLVLSLP 200

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:cd00919    86 NNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMT 165

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:cd00919   166 LDKMPLFVWSVLVTAILLLLALP 188

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:cd01662    92 NALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT 171

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:cd01662   172 LMRMPIFTWTTLVTSILILFAFP 194

cytochrome c oxidase subunit I; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778  24 GAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMSLdQTPLFVWAVGITALL*LLSLP 103
Cdd:MTH00048  120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1070697778   1 NNMSFWLLPPSLTLLLASSMVENGAGTGWTVYPPLSANIAHAGASVDLAIFSLHLAGISSILGAVNFITTTINMRAPGMS 80
Cdd:TIGR02882 135 NALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMK 214

                          90       100
                  ....*....|....*....|...
gi 1070697778  81 LDQTPLFVWAVGITALL*LLSLP 103
Cdd:TIGR02882 215 LMQMPMFTWTTLITTLIIIFAFP 237