The 3 Terminal Oxidase of

Giuffrè, Alessandro; D’Itri, Emilio; Giannini, Silva; Brunori, Maurizio; Ubbink-Kok, Trees; Konings, Wil N.; Antonini, Giovanni

doi:10.1074/jbc.271.24.13987

Cited by 5 publications

(3 citation statements)

References 29 publications

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“…In the R. sphaeroides and bovine enzymes, this reaction step is also associated with rereduction of heme a by Cu A . In the R. marinus enzyme, the situation is more complicated as Cu A is in rapid equilibrium with the bound heme c [see also (30,31)]. This is why there is essentially no net oxidation of Cu A (no change in absorbance at 830 nm on the time scale of F formation), and a decrease in absorbance is seen at 550 nm, associated with oxidation of heme c. The heme a reduction and proton uptake from the bulk solution during P r f F are detected as an increase in absorbance at 605/445 and 560 nm, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…In the R . marinus enzyme, the situation is more complicated as Cu A is in rapid equilibrium with the bound heme c [see also ( , )]. This is why there is essentially no net oxidation of Cu A (no change in absorbance at 830 nm on the time scale of F formation), and a decrease in absorbance is seen at 550 nm, associated with oxidation of heme c .…”

Section: Discussionmentioning

confidence: 99%

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Ligand Binding and the Catalytic Reaction of Cytochrome caa₃ from the Thermophilic Bacterium Rhodothermus marinus

et al. 2001

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The ligand-binding dynamics and the reaction with O(2) of the fully (five-electron) reduced cytochrome caa(3) from the thermohalophilic bacterium Rhodothermus (R.) marinus were investigated. The enzyme is a proton pump which has all the residues of the proton-transfer pathways found in the mitochondrial-like enzymes conserved, except for one of the key elements of the D-pathway, the helix-VI glutamate [Glu(I-286), R. sphaeroides numbering]. In contrast to what has been suggested previously as general characteristics of thermophilic enzymes, during formation of the R. marinus caa(3)-CO complex, CO binds weakly to Cu(B), and is rapidly (k(Ba) = 450 s(-1)) trapped by irreversible (K(Ba) = 4.5 x 10(3)) binding to heme a(3). Upon reaction of the fully reduced enzyme with O(2), four kinetic phases were resolved during the first 10 ms after initiation of the reaction. On the basis of a comparison to reactions observed with the bovine enzyme, these phases were attributed to the following transitions between intermediates (pH 7.8, 1 mM O(2)): R --> A (tau congruent with 8 micros), A --> P(r) (tau congruent with 35 micros), P(r) --> F (tau congruent with 240 micros), F --> O (tau congruent with 2.5 ms), where the last two phases were associated with proton uptake from the bulk solution. Oxidation of heme c was observed only during the last two reaction steps. The slower transition times as compared to those observed with the bovine enzyme most likely reflect the replacement of Glu(I-286) of the helix-VI motif -XGHPEV- by a tyrosine in the R. marinus enzyme in the motif -YSHPXV-. The presence of an additional, fifth electron in the enzyme was reflected by two additional kinetic phases with time constants of approximately 20 and approximately 720 ms during which the fifth electron reequilibrated within the enzyme.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Ligand Binding and the Catalytic Reaction of Cytochrome caa₃ from the Thermophilic Bacterium Rhodothermus marinus

et al. 2001

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“…The HCO is further divided into three families: A, B and C (Wikströ m and Verkhovsky, 2007;Borisov et al, 2011;Lee et al, 2012). The A-family includes the aa 3 -type cytochrome c oxidase such as that in Paracoccus denitrificans (caa 3 -type in some cases, the aa 3 -type enzymes with a c heme-containing domain, as observed in Bacillus stearothermophilus) and the bo 3 -type quinol oxidase as in Escherichia coli (Puustinen et al, 1991;Giuffrè et al, 1996;Baker et al, 1998). The B-family includes a number of oxidases from extremophilic prokaryotes, such as the ba 3 -type enzyme of Thermus thermophilus (Chang et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Combined effect of loss of the caa3 oxidase and Crp regulation drives Shewanella to thrive in redox-stratified environments

et al. 2013

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Shewanella species are a group of facultative Gram-negative microorganisms with remarkable respiration abilities that allow the use of a diverse array of terminal electron acceptors (EA). Like most bacteria, S. oneidensis possesses multiple terminal oxidases, including two heme-copper oxidases (caa 3 -and cbb 3 -type) and a bd-type quinol oxidase. As aerobic respiration is energetically favored, mechanisms underlying the fact that these microorganisms thrive in redox-stratified environments remain vastly unexplored. In this work, we discovered that the cbb 3 -type oxidase is the predominant system for respiration of oxygen (O 2 ), especially when O 2 is abundant. Under microaerobic conditions, the bd-type quinol oxidase has a significant role in addition to the cbb 3 -type oxidase. In contrast, multiple lines of evidence suggest that under test conditions the caa 3 -type oxidase, an analog to the mitochondrial enzyme, has no physiological significance, likely because of its extremely low expression. In addition, expression of both cbb 3 -and bd-type oxidases is under direct control of Crp (cAMP receptor protein) but not the well-established redox regulator Fnr (fumarate nitrate regulator) of canonical systems typified in Escherichia coli. These data, collectively, suggest that adaptation of S. oneidensis to redox-stratified environments is likely due to functional loss of the caa 3 -type oxidase and switch of the regulatory system for respiration.

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The fifth electron in the fully reduced caa3 from Thermus thermophilus is competent in proton pumping

Siletsky

Belevich

Soulimane

et al. 2013

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The time-resolved kinetics of membrane potential generation coupled to oxidation of the fully reduced (five-electron) caa(3) cytochrome oxidase from Thermus thermophilus by oxygen was studied in a single-turnover regime. In order to calibrate the number of charges that move across the vesicle membrane in the different reaction steps, the reverse electron transfer from heme a(3) to heme a and further to the cytochrome c/Cu(A) has been resolved upon photodissociation of CO from the mixed valence enzyme in the absence of oxygen. The reverse electron transfer from heme a(3) to heme a and further to the cytochrome c/Cu(A) pair is resolved as a single transition with τ~40 μs. In the reaction of the fully reduced cytochrome caa(3) with oxygen, the first electrogenic phase (τ~30 μs) is linked to OO bond cleavage and generation of the P(R) state. The next electrogenic component (τ~50 μs) is associated with the P(R)→F transition and together with the previous reaction step it is coupled to translocation of about two charges across the membrane. The three subsequent electrogenic phases, with time constants of ~0.25 ms, ~1.4 ms and ~4 ms, are linked to the conversion of the binuclear center through the F→O(H)→E(H) transitions, and result in additional transfer of four charges through the membrane dielectric. This indicates that the delivery of the fifth electron from heme c to the binuclear center is coupled to pumping of an additional proton across the membrane.

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The 3 Terminal Oxidase of

Cited by 5 publications

References 29 publications

Ligand Binding and the Catalytic Reaction of Cytochrome caa₃ from the Thermophilic Bacterium Rhodothermus marinus

Ligand Binding and the Catalytic Reaction of Cytochrome caa₃ from the Thermophilic Bacterium Rhodothermus marinus

Combined effect of loss of the caa3 oxidase and Crp regulation drives Shewanella to thrive in redox-stratified environments

The fifth electron in the fully reduced caa3 from Thermus thermophilus is competent in proton pumping

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The 3 Terminal Oxidase of

Cited by 5 publications

References 29 publications

Ligand Binding and the Catalytic Reaction of Cytochrome caa3 from the Thermophilic Bacterium Rhodothermus marinus

Ligand Binding and the Catalytic Reaction of Cytochrome caa3 from the Thermophilic Bacterium Rhodothermus marinus

Combined effect of loss of the caa3 oxidase and Crp regulation drives Shewanella to thrive in redox-stratified environments

The fifth electron in the fully reduced caa3 from Thermus thermophilus is competent in proton pumping

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Ligand Binding and the Catalytic Reaction of Cytochrome caa₃ from the Thermophilic Bacterium Rhodothermus marinus

Ligand Binding and the Catalytic Reaction of Cytochrome caa₃ from the Thermophilic Bacterium Rhodothermus marinus