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Ns-?s Time-Resolved Step-Scan FTIR of ba? Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927.

ABSTRACT: Time-resolved step-scan FTIR spectroscopy has been employed to probe the dynamics of the ba? oxidoreductase from Thermus thermophilus in the ns-?s time range and in the pH/pD 6-9 range. The data revealed a pH/pD sensitivity of the D372 residue and of the ring-A propionate of heme a?. Based on the observed transient changes a model in which the protonic connectivity of w941-w946-927 to the D372 and the ring-A propionate of heme a? is described.

SUBMITTER: Nicolaides A

PROVIDER: S-EPMC5085690 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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ns-μs Time-Resolved Step-Scan FTIR of ba₃ Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927.

Nicolaides Antonis A Soulimane Tewfik T Varotsis Constantinos C

International journal of molecular sciences 20160929 10

Time-resolved step-scan FTIR spectroscopy has been employed to probe the dynamics of the ba₃ oxidoreductase from Thermus thermophilus in the ns-μs time range and in the pH/pD 6-9 range. The data revealed a pH/pD sensitivity of the D372 residue and of the ring-A propionate of heme a₃. Based on the observed transient changes a model in which the protonic connectivity of w941-w946-927 to the D372 and the ring-A propionate of heme a₃ is described. ...[more]

PMID: 27690021

Similar Datasets

Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba3-cytochrome c oxidase from Thermus thermophilus: a Fourier transform infrared (FTIR) and time-resolved step-scan FTIR study.

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Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus.

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Thiostrepton-resistant mutants of Thermus thermophilus.

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