Human serum albumin mutants complexed Mn(III) protoporphyrin IX as superoxide dismutase mimics

Genetically engineered human serum albumin (HSA) mutants complexed Mn(III) protoporphyrin IX (MnPP) in the haem pocket showed superoxide dismutase activity. Replacement of a proximal Tyr-161 by non-coordinating Leu caused a remarkable increase in enzyme activity.

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Bibliographic Details
Published in:Dalton transactions : an international journal of inorganic chemistry 2013-12, Vol.42 (45), p.15889-15892
Main Authors: Kato, Ryunosuke, Kobayashi, Yuya, Akiyama, Motofusa, Komatsu, Teruyuki
Format: Article
Language:English
Subjects:
Coordination Complexes - chemistry
Humans
Manganese - chemistry
Models, Molecular
Mutagenesis, Site-Directed
Point Mutation
Protoporphyrins - chemistry
Serum Albumin - chemistry
Serum Albumin - genetics
Serum Albumin - metabolism
Superoxide Dismutase - metabolism
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Summary:Genetically engineered human serum albumin (HSA) mutants complexed Mn(III) protoporphyrin IX (MnPP) in the haem pocket showed superoxide dismutase activity. Replacement of a proximal Tyr-161 by non-coordinating Leu caused a remarkable increase in enzyme activity.
ISSN:1477-9226
1477-9234
DOI:10.1039/c3dt51418h