Cytochrome c oxidase in prokaryotes

Ludwig, Bernd

doi:10.1016/0378-1097(87)90185-6

Cited by 48 publications

(62 citation statements)

References 68 publications

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“…This is not so, however, if procaryotes are considered which are not closely related to the purple bacteria group. Since several of these are aerobes, a multiple origin of O2 respiration [7] and thus different terminal oxidases [34] seemed to be plausible. Thermus has been included in the 16-S rRNA investigations and its branching from other bacterial divisions found among the earliest of eubacteria [32].…”

Section: V-t-g-y-q-f T-t-r-i-s-f 7 A-a-k-a-s-p-h-p-v-a-d-e-r-g-q-q-v-mentioning

confidence: 99%

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c₁aa₃’ of Thermus thermophilus

Buse

Hensel

Fee

1989

European Journal of Biochemistry

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The terminal cytochrome claa3 of the respiratory chain of Thermus thermophilus has been isolated and purified to homogeneity by a novel procedure. The two subunit proteins (55 and 33 kDa) have been characterized chemically. Computer searches with partial amino acid sequences obtained from both subunits show that the larger subunit belongs to the cytochrome oxidase subunit I protein family while the smaller covalently hemebinding subunit is not a cytochrome c1 but appears to be a fused protein between cytochrome c and cytochrome oxidase subunit 11.With respect to the 16-S rRNA-derived phylogeny of procaryotes, the results show that the genetic information for an 02-reacting cytochrome oxidase (EC 1.9.3.1) existed already in early eubacteria.Respiratory chains of many bacteria contain terminal 02-reducing oxidases with similar spectroscopic and functional properties but much simpler subunit structure than the mitochondrial cytochrome-c oxidase (EC 1.9.3.1) [I -31. Thus the enzyme from the plasma membrane of Paracoccus denitrificans can either be isolated as a functional (02-reducing and H+-pumping) two-or three-subunit complex homologous to the mtDNA-coded subunits I, I1 and eventually 111 of the mitochondrial enzyme [4, 51. From these data it had been inferred that subunits I and 11 represent a minimum catalytic structure capable of binding the canonical four metal centers (heme a, heme u3, CuA and CuB) and of catalysing the reaction 4Cytc" + O2 + (4 + n)H' = 4Cytc3+ + 2H2O + nH:where i and o refer to the inner and outer sites of the membrane. Furthermore, the sequence analyses with the Paracoccus enzyme have suggested that this bacterium is a descendant from those ancient bacteria from which eucaryotic mitochondria also originated under the selection pressure of a rising oxygen atmosphere [6]. The origin of more distantly related aerobic bacterial lines is, however, assumed to fall beyond the earths' O2 horizon and, consequently, it has been argued that O2 respiration evolved several times independently [7].Recently a terminal claa3 oxidase from the strictly aerobic bacterium Thermus thermophilus has been described [8, 91

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Section: V-t-g-y-q-f T-t-r-i-s-f 7 A-a-k-a-s-p-h-p-v-a-d-e-r-g-q-q-v-mentioning

confidence: 99%

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c₁aa₃’ of Thermus thermophilus

Buse

Hensel

Fee

1989

European Journal of Biochemistry

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“…Therefore, it was of interest to find out whether proton slippage was an intrinsic property of the catalytic core of COX, composed of the mitochondrial-encoded subunits I and 11, or was due to the nuclear-encoded subunits, which are absent in COX from bacteria. Isolated COX from Paracoccus denitrificans contains either two or three subunits, which are homologeous to the mitochondrial-encoded subunits I-I11 of mammalian COX (Ludwig, 1987). In previous studies, it was assumed that subunit I11 may have an important role in the proton pumping capability of COX (see Prochaska and Fink, 1987, for review).…”

mentioning

confidence: 99%

Proton slippage in cytochrome c oxidase of Paracoccus denitrificans

Steverding

Köhnke

Ludwig

et al. 1993

European Journal of Biochemistry

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Isolated cytochrome c oxidase from Paracoccus denitrzjkans, containing either two or three subunits, was reconstituted into liposomes and the membrane potential was measured at different rates of respiration using a triphenylmethylphosponium bromide electrode. Both enzymes revealed a non-linear increase of the membrane potential with increasing respiratory rates. The ratios of the respiratory rates of the two proton pumps decreased with increasing membrane potential, suggesting slippage of proton pumping, as has been shown before with two cytochrome c oxidases from bovine heart, differing in H+/e-stoichiometries due to chemical modification The generally observed non-linear relationship between electron-transfer rates and the proton motive force (ApH', or the membrane potential in the presence of the H+/ K'antiporter, nigericin) of redox proton pumps was explained either by the dpH+ dependence of the membrane H+-leak conductance (O'Shea et al., 1984;Krishnamoorthy and Hinkle, 1984;Murphy and Brand, 1987;Hafner and Brand, 1991 ;Brown and Brand, 1991), or, at least in part, by a variable (membrane-potential dependent) H+/e-stoichiametry (slippage of proton pumps; Pietrobon et al., 1981Pietrobon et al., , 1983Zoratti et al., 1986). In a recent publication, we could support proton slippage in cytochrome c oxidase (COX) by measuring the ratio of electron-transfer rates of two different efficient proton pumps at various membrane potentials (Steverding and Kadenbach, 1991). COX from bovine heart was reduced in proton pumping efficiency by chemical modification with N-ethoxycarbonyl-2-ethoxy-1 ,Zdihydroquinoline. The observed decrease in the ratio of electron-transfer rates of the two proton pumps with increasing membrane potential was taken to indicate proton slippage in reconstituted COX from bovine heart.Mammalian COX contains three mitochondrial-encoded and ten nuclear-encoded subunits . Therefore, it was of interest to find out whether proton slippage was an intrinsic property of the catalytic core of COX, composed of the mitochondrial-encoded subunits I and 11, or was due to the nuclear-encoded subunits, which are absent in COX from bacteria. Isolated COX from Paracoccus denitrificans contains either two or three subunits, which are Correspondence to

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“…These three subunits show immunological cross-reactivity with antibodies raised against the corresponding subunits of the mammalian enzyme, as well as significant sequence homology. The three-subunit P. denitrificans enzyme contains all of the redox active metal cofactor and displays electron transfer and proton translocation activity similar to the mammalian enzyme (Ludwig, 1987). In this study we compare the spectroscopic features of the 1 : 1 complexes between cytochrome c and the cytochrome c oxidase from two evolutionarily diverse species, bovine (Bos taurus) and P. denitrificans.…”

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confidence: 99%

Electronic and vibrational spectroscopy of the cytochrome c: Cytochrome c oxidase complexes from bovine and Paracoccus denitrificans

Lynch¹,

Copeland²

1992

Protein Science

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The 1: 1 complex between horse heart cytochrome c and bovine cytochrome c oxidase, and between yeast cytochrome c and Paracoccus denitrificans cytochrome c oxidase have been studied by a combination of second derivative absorption, circular dichroism (CD), and resonance Raman spectroscopy. The second derivative absorption and CD spectra reveal changes in the electronic transitions of cytochrome a upon complex formation. These results could reflect changes in ground state heme structure or changes in the protein environment surrounding the chromophore that affect either the ground or excited electronic states. The resonance Raman spectrum, on the other hand, reflects the heme structure in the ground electronic state only and shows no significant difference between cytochrome a vibrations in the complex or free enzyme. The only major difference between the Raman spectra of the free enzyme and complex is a broadening of the cytochrome a3 formyl band of the complex that is relieved upon complex dissociation at high ionic strength. These data suggest that the differences observed in the second derivative and CD spectra are the result of changes in the protein environment around cytochrome a that affect the electronic excited state. By analogy to other protein-chromophore systems, we suggest that the energy of the Soret "K* state of cytochrome a may be affected by (1) changes in the local dielectric, possibly brought about by movement of a charged amino acid side chain in proximity to the heme group, or (2) T-"K interactions between the heme and aromatic amino acid residues.

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Cytochrome c oxidase in prokaryotes

Cited by 48 publications

References 68 publications

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c₁aa₃’ of Thermus thermophilus

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c₁aa₃’ of Thermus thermophilus

Proton slippage in cytochrome c oxidase of Paracoccus denitrificans

Electronic and vibrational spectroscopy of the cytochrome c: Cytochrome c oxidase complexes from bovine and Paracoccus denitrificans

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Cytochrome c oxidase in prokaryotes

Cited by 48 publications

References 68 publications

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c1aa3’ of Thermus thermophilus

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c1aa3’ of Thermus thermophilus

Proton slippage in cytochrome c oxidase of Paracoccus denitrificans

Electronic and vibrational spectroscopy of the cytochrome c: Cytochrome c oxidase complexes from bovine and Paracoccus denitrificans

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Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c₁aa₃’ of Thermus thermophilus

Evidence for cytochrome oxidase subunit I and a cytochrome c– subunit II fused protein in the cytochrome ‘c₁aa₃’ of Thermus thermophilus