FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum

Michael J.K. Nelson; David P. Brown; James G. Ferry

doi:10.1016/S0006-291X(84)80174-6

FAD requirement for the reduction of coenzyme F₄₂₀ by hydrogenase from Methanobacterium formicicum

Michael J.K. Nelson, David P. Brown, James G. Ferry

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Hydrophobic interaction chromatography of coenzyme F₄₂₀-reducing hydrogenase purified from Methanobacterium formicicum depleted protein-bound FAD and eliminated the ability to reduce coenzyme F₄₂₀. Preincubation of the FAD-depleted hydrogenase with FAD restored 85% of the coenzyme F₄₂₀-reducing activity. FMN did not replace FAD. A Kd of 12 μM was estimated for FAD. Analysis of the reactivated hydrogenase following molecular sieve column chromatography showed that FAD was bound to protein. The results indicate that protein-bound FAD is reversibly removed from the coenzyme F₄₂₀-reducing hydrogenase and that this flavin is required for the reduction of coenzyme F₄₂₀.

Original language	English (US)
Pages (from-to)	775-781
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	120
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(84)80174-6
State	Published - May 16 1984

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/S0006-291X(84)80174-6

Cite this

@article{3e722ff67677464186c7a166e1acf91e,

title = "FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum",

abstract = "Hydrophobic interaction chromatography of coenzyme F420-reducing hydrogenase purified from Methanobacterium formicicum depleted protein-bound FAD and eliminated the ability to reduce coenzyme F420. Preincubation of the FAD-depleted hydrogenase with FAD restored 85% of the coenzyme F420-reducing activity. FMN did not replace FAD. A Kd of 12 μM was estimated for FAD. Analysis of the reactivated hydrogenase following molecular sieve column chromatography showed that FAD was bound to protein. The results indicate that protein-bound FAD is reversibly removed from the coenzyme F420-reducing hydrogenase and that this flavin is required for the reduction of coenzyme F420.",

author = "Nelson, {Michael J.K.} and Brown, {David P.} and Ferry, {James G.}",

note = "Funding Information: *This work was supported by National Science Foundation grant PCM 7812148 AOI. We are grateful to Nell L. Schauer for valuable discussions and advice. We wish to thank Robert Hausinger for the nickel and iron analyses. (This work was reported in part at the 84th Annual Meeting of the American Society for Microbiology, St. Louis, MO, 5-9 March 1984.) Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1984",

month = may,

day = "16",

doi = "10.1016/S0006-291X(84)80174-6",

language = "English (US)",

volume = "120",

pages = "775--781",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum

AU - Nelson, Michael J.K.

AU - Brown, David P.

AU - Ferry, James G.

N1 - Funding Information: *This work was supported by National Science Foundation grant PCM 7812148 AOI. We are grateful to Nell L. Schauer for valuable discussions and advice. We wish to thank Robert Hausinger for the nickel and iron analyses. (This work was reported in part at the 84th Annual Meeting of the American Society for Microbiology, St. Louis, MO, 5-9 March 1984.) Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1984/5/16

Y1 - 1984/5/16

N2 - Hydrophobic interaction chromatography of coenzyme F420-reducing hydrogenase purified from Methanobacterium formicicum depleted protein-bound FAD and eliminated the ability to reduce coenzyme F420. Preincubation of the FAD-depleted hydrogenase with FAD restored 85% of the coenzyme F420-reducing activity. FMN did not replace FAD. A Kd of 12 μM was estimated for FAD. Analysis of the reactivated hydrogenase following molecular sieve column chromatography showed that FAD was bound to protein. The results indicate that protein-bound FAD is reversibly removed from the coenzyme F420-reducing hydrogenase and that this flavin is required for the reduction of coenzyme F420.

AB - Hydrophobic interaction chromatography of coenzyme F420-reducing hydrogenase purified from Methanobacterium formicicum depleted protein-bound FAD and eliminated the ability to reduce coenzyme F420. Preincubation of the FAD-depleted hydrogenase with FAD restored 85% of the coenzyme F420-reducing activity. FMN did not replace FAD. A Kd of 12 μM was estimated for FAD. Analysis of the reactivated hydrogenase following molecular sieve column chromatography showed that FAD was bound to protein. The results indicate that protein-bound FAD is reversibly removed from the coenzyme F420-reducing hydrogenase and that this flavin is required for the reduction of coenzyme F420.

UR - http://www.scopus.com/inward/record.url?scp=0021765275&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021765275&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(84)80174-6

DO - 10.1016/S0006-291X(84)80174-6

M3 - Article

C2 - 6375661

AN - SCOPUS:0021765275

SN - 0006-291X

VL - 120

SP - 775

EP - 781

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

FAD requirement for the reduction of coenzyme F₄₂₀ by hydrogenase from Methanobacterium formicicum

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this