Please use this identifier to cite or link to this item: https://doi.org/10.1006/bbrc.1996.0899
DC FieldValue
dc.titleTotal synthesis of a miniferredoxin
dc.contributor.authorSow, T.-C.
dc.contributor.authorPedersen, M.V.
dc.contributor.authorChristensen, H.E.M.
dc.contributor.authorOoi, B.-L.
dc.date.accessioned2014-11-28T08:12:34Z
dc.date.available2014-11-28T08:12:34Z
dc.date.issued1996-06-14
dc.identifier.citationSow, T.-C., Pedersen, M.V., Christensen, H.E.M., Ooi, B.-L. (1996-06-14). Total synthesis of a miniferredoxin. Biochemical and Biophysical Research Communications 223 (2) : 360-364. ScholarBank@NUS Repository. https://doi.org/10.1006/bbrc.1996.0899
dc.identifier.issn0006291X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/112947
dc.description.abstractA miniferredoxin has been designed based on the Desulfovibrio gigas ferredoxin II structure and has been successfully synthesized. The 31 amino acid apoprotein was synthesized via standard Fmoc solid phase peptide synthesis and in vitro cluster insertion carried out. The UV-visible spectrum of the miniferredoxin (peak at 300 nm and a shoulder at 405 nm) shows the same features as that of the D. gigas ferredoxin. Cyclic voltammetry indicated a quasireversible electrode process with a midpoint potential of -370 mV vs NHE, which demonstrates that the miniferredoxin is redox active. From these and EPR studies, we propose the incorporation of a Fe4S4 cluster.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1006/bbrc.1996.0899
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMISTRY
dc.contributor.departmentINSTITUTE OF MOLECULAR AGROBIOLOGY
dc.description.doi10.1006/bbrc.1996.0899
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume223
dc.description.issue2
dc.description.page360-364
dc.description.codenBBRCA
dc.identifier.isiutA1996UR69600028
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