Kinetic and Ligand Binding Evidence for Two Heme A-Based Terminal Oxidases in Plasma Membranes from Bacillus subtilis

Hill, Bruce C.; Vo, Luan; Albanese, Joseph A.

doi:10.1006/abbi.1993.1124

Cited by 6 publications

(9 citation statements)

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“…The remaining cytochrome aa 3 content is due to the presence of menaquinol oxidase. This change is in keeping with our previous estimate of the cytochrome c oxidase and menaquinol oxidase contents in wild type cells (38) and the loss of cytochrome c oxidase in BH144 (⌬ypmQ). When the growth medium is supplemented with copper the cytochrome caa 3 content of BH144 is increased to 21% that of wild type.…”

Section: јAgcaatcacttggtcctctccct3јsupporting

confidence: 92%

“…Furthermore, more than 90% of the flux from ascorbate plus TMPD is carried by cytochrome c oxidase. The steady-state cytochrome c oxidase activity of the wild type extract is similar to that reported previously (38). The apparent activity of BH144 grown on low copper media is reduced 25-fold relative to the wild type extract (Table III).…”

Section: јAgcaatcacttggtcctctccct3јsupporting

confidence: 85%

“…In each trace the oxidized level of the sample was measured prior to addition of the reductants, ascorbate and TMPD, which produce a steady-state level of reduction until the dissolved O 2 is completely consumed at which time the absorption increases rapidly to full reduction. We have shown previously that aerobic cultures of B. subtilis contain two components that are reduced in this assay, namely cytochrome c oxidase and menaquinol oxidase (38). Furthermore, more than 90% of the flux from ascorbate plus TMPD is carried by cytochrome c oxidase.…”

Section: јAgcaatcacttggtcctctccct3јmentioning

confidence: 72%

“…YpmQ, an Assembly Factor for Cytochrome c Oxidasetant to note that TMPD is a poor electron donor to menaquinol oxidase, the other heme A-based terminal oxidase present in membrane extracts of B. subtilis (38). Fig.…”

Section: јAgcaatcacttggtcctctccct3јmentioning

confidence: 99%

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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

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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.

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Section: јAgcaatcacttggtcctctccct3јsupporting

confidence: 92%

Section: јAgcaatcacttggtcctctccct3јsupporting

confidence: 85%

Section: јAgcaatcacttggtcctctccct3јmentioning

confidence: 72%

Section: јAgcaatcacttggtcctctccct3јmentioning

confidence: 99%

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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

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“…Purification of cytochrome c oxidase from Bacillus subtilis, reported originally by de Vrij et al [5], describes an aa3-type oxidase that can oxidize cytochrome c. However, subsequent genetic [3,4] and biochemical [6,7] studies have demonstrated that the cytochrome c-oxidizing activity ofBacillus subtilis plasma membranes is associated with the cytochrome caa3 oxidase. The enzyme with the spectral features reported by de Vrij et al [5] resembles more closely the cytochrome aa3-quinol oxidase.…”

Section: Introductionmentioning

confidence: 99%

High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes

Henning

Albanese

et al. 1995

Biochemical Journal

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When grown in aerated shaking culture, Bacillus subtilis expresses two different haem A-containing terminal oxidases: cytochrome aa3-quinol oxidase and cytochrome caa3 oxidase. This paper describes a high-yield conventional procedure for purifying the two haem A-containing oxidases from the same aerobic culture of Bacillus subtilis. Yields of close to 40% of the total haem A are achieved and about 6 mg of each of the purified oxidases is obtained from 4 litres of liquid culture. Both of the purified enzymes have two subunits, with apparent molecular masses of 71.6 kDa and 34.3 kDa for the cytochrome caa3 oxidase, and 67.6 kDa and 37.2 kDa for aa3-quinol oxidase. These features are in agreement with the sequence data for the corresponding structural genes in the aa3 and caa3 operons of B. subtilis. Some spectral and enzymic features of the two purified oxidases are reported that are consistent with the inclusion of both of these enzymes as members of the cytochrome oxidase superfamily.

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Stopped-Flow, Laser-Flash Photolysis Studies on the Reactions of CO and O₂ with the Cytochrome caa₃ Complex from Bacillus subtilis: Conservation of Electron Transfer Pathways from Cytochrome c to O₂

Hill

1996

Biochemistry

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The reaction of CO and O2 with fully reduced cytochrome caa3 from Bacillus subtilis has been studied by rapid reaction spectrophotometry. The fully reduced caa3 complex reacts with CO to give a spectrum that is characteristic of formation of ferrocytochrome a3-CO. This adduct is photosensitive, and its recombination rate is proportional to CO concentration with a bimolecular value of 1.2 x 10(5)M-1 s-1. When the CO compound of the reduced complex is exposed to O2, the rate of oxidation proceeds at 0.1 s-1, which is assigned as the CO off rate. These kinetic constants give an equilibrium dissociation constant for the CO complex of 0.83 microM. Photolysis of the CO adduct in the presence of O2 reveals three reaction phases over the first 3 ms and an additional phase on the second time scale. A kinetic model is proposed in which fully reduced oxidase first combines with O2 and then electron transfer commences from both cytochrome a and a3, followed rapidly by electron input from CuA and the cytochrome c domain. An equivalent kinetic model has been used to account for the reactivity of mammalian cytochrome c oxidase in its electrostatic complex with soluble cytochrome c [Hill, B. C., (1994) J. Biol. Chem. 269, 2419-2425]. However, unlike the mitochondrial complex, the reactivity of cytochrome c in the B. subtilis caa3 complex is unaffected by ionic strength. Thus the cytochrome c moiety in the B. subtilis caa3 complex seems to be fixed in a reactive orientation by its covalent association with the rest of the oxidase complex. The pathway of electron transfer from cytochrome c to O2 appears very well conserved from B. subtilis to the mammalian respiratory chain, making the B. subtilis protein a good model to probe intersite electron transfer within the cytochrome c-cytochrome oxidase complex.

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Kinetic and Ligand Binding Evidence for Two Heme A-Based Terminal Oxidases in Plasma Membranes from Bacillus subtilis

Cited by 6 publications

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

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

High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes

Stopped-Flow, Laser-Flash Photolysis Studies on the Reactions of CO and O₂ with the Cytochrome caa₃ Complex from Bacillus subtilis: Conservation of Electron Transfer Pathways from Cytochrome c to O₂

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Kinetic and Ligand Binding Evidence for Two Heme A-Based Terminal Oxidases in Plasma Membranes from Bacillus subtilis

Cited by 6 publications

References 0 publications

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

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

High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes

Stopped-Flow, Laser-Flash Photolysis Studies on the Reactions of CO and O2 with the Cytochrome caa3 Complex from Bacillus subtilis: Conservation of Electron Transfer Pathways from Cytochrome c to O2

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Stopped-Flow, Laser-Flash Photolysis Studies on the Reactions of CO and O₂ with the Cytochrome caa₃ Complex from Bacillus subtilis: Conservation of Electron Transfer Pathways from Cytochrome c to O₂