Characterization of a novel cytochrome c as the electron acceptor of XoxF-MDH in the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV.

Authors:
Wouter Versantvoort
Wouter Versantvoort
Institute for Water and Wetland Research
Arjan Pol
Arjan Pol
Radboud University Nijmegen
Netherlands
Lena J Daumann
Lena J Daumann
The University of Queensland
Australia
James A Larrabee
James A Larrabee
Middlebury College
Middlebury | United States
Laura van Niftrik
Laura van Niftrik
Radboud University of Nijmegen
Netherlands
Joachim Reimann
Joachim Reimann
Stockholm University
Sweden

Biochim Biophys Acta Proteins Proteom 2019 Jun 4;1867(6):595-603. Epub 2019 Apr 4.

Department of Microbiology, IWWR, Radboud University, Heyendaalseweg, 135 6525, AJ, Nijmegen, the Netherlands. Electronic address:

Methanotrophs play a prominent role in the global carbon cycle, by oxidizing the potent greenhouse gas methane to CO. Methane is first converted into methanol by methane monooxygenase. This methanol is subsequently oxidized by either a calcium-dependent MxaF-type or a lanthanide-dependent XoxF-type methanol dehydrogenase (MDH). Electrons from methanol oxidation are shuttled to a cytochrome redox partner, termed cytochrome c. Here, the cytochrome c homolog from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV was characterized. SolV cytochrome c is a fusion of a XoxG cytochrome and a periplasmic binding protein XoxJ. Here we show that XoxGJ functions as the direct electron acceptor of its corresponding XoxF-type MDH and can sustain methanol turnover, when a secondary cytochrome is present as final electron acceptor. SolV cytochrome c (XoxGJ) further displays a unique, red-shifted absorbance spectrum, with a Soret and Q bands at 440, 553 and 595 nm in the reduced state, respectively. VTVH-MCD spectroscopy revealed the presence of a low spin iron heme and the data further shows that the heme group exhibits minimal ruffling. The midpoint potential E of +240 mV is similar to other cytochrome c type proteins but remarkably, the midpoint potential of cytochrome c was not influenced by lowering the pH. Cytochrome c represents the first example of a cytochrome from a strictly lanthanide-dependent methylotrophic microorganism.

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http://dx.doi.org/10.1016/j.bbapap.2019.04.001DOI Listing

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June 2019
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