Nitrite reductase activity in F420-dependent sulphite reductase (Fsr) from Methanocaldococcus jannaschii

Author:

Heryakusuma Christian12,Johnson Eric F.1,Purwantini Endang1,Mukhopadhyay Biswarup321ORCID

Affiliation:

1. Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA

2. Genetics, Bioinformatics, and Computational Biology Ph.D. Program, Virginia Tech, Blacksburg, VA 24061, USA

3. Virginia Tech Carilion School of Medicine, Virginia Tech, Blacksburg, VA 24061, USA

Abstract

Methanocaldococcus jannaschii (Mj), a hyperthermophilic and evolutionarily deeply rooted methanogenic archaeon from a deep-sea hydrothermal vent, produces F420-dependent sulphite reductase (Fsr) in response to exposure to sulphite. This enzyme allows Mj to detoxify sulphite, a potent inhibitor of methyl coenzyme-M reductase (Mcr), by reducing it to sulphide with reduced coenzyme F420 (F420H2) as an electron donor; Mcr is essential for energy production for a methanogen. Fsr allows Mj to utilize sulphite as a sulphur source. Nitrite is another potent inhibitor of Mcr and is toxic to methanogens. It is reduced by most sulphite reductases. In this study, we report that MjFsr reduced nitrite to ammonia with F420H2 with physiologically relevant K m values (nitrite, 8.9 µM; F420H2, 9.7 µM). The enzyme also reduced hydroxylamine with a K m value of 112.4 µM, indicating that it was an intermediate in the reduction of nitrite to ammonia. These results open the possibility that Mj could use nitrite as a nitrogen source if it is provided at a low concentration of the type that occurs in its habitat.

Funder

NASA Headquarters

Virginia Tech Agricultural Experiment Station Hatch Program of National Institute of Food and Agriculture of the United States Department of Agriculture

Publisher

Microbiology Society

Subject

Microbiology (medical),Microbiology

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