A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as 
deduced from studies with subunit B of heterodisulfide reductase from 
methanothermobacter marburgensis

Hamann, N.; Mander, G. J.; Shokes, J. E.; Scott, R.; Bennati, M.; Hedderich, R.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from methanothermobacter marburgensis

MPS-Authors

/persons/resource/persons14834

Bennati, M.
Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Hamann, N., Mander, G. J., Shokes, J. E., Scott, R., Bennati, M., & Hedderich, R. (2007). A cysteine-rich CCG domain contains a novel [4Fe-4S] cluster binding motif as deduced from studies with subunit B of heterodisulfide reductase from methanothermobacter marburgensis. Biochemistry, 46(44), 12875-12885. Retrieved from http://pubs.acs.org/cgi-bin/article.cgi/bichaw/2007/46/i44/pdf/bi700679u.pdf.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-DEDF-2

Abstract

There is no abstract available