New functionalization of myoglobin by chemical modification of heme-propionates

Takashi Hayashi, Yoshio Hisaeda

Research output: Contribution to journalArticle

158 Citations (Scopus)

Abstract

The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. Particularly, the modification of two heme-propionates gives us an effective binding domain or binding site on the protein surface. This Account traces the design and construction of the highly ordered binding domain around the entrance of the heme pocket. The discussion includes the protein-small molecule or protein-protein recognition, electron transfer reaction within the complex, and enhancement of the chemical reactivity of the myoglobin with a substrate binding site. The synthetic approach to modifying a protein will be a new trend in engineering a novel function in naturally occurring hemoprotein.

Original languageEnglish
Pages (from-to)35-43
Number of pages9
JournalAccounts of Chemical Research
Volume35
Issue number1
DOIs
Publication statusPublished - Jan 31 2002
Externally publishedYes

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Myoglobin
Propionates
Chemical modification
Heme
Proteins
Binding Sites
Chemical reactivity
Prosthetics
Membrane Proteins
Molecules
Electrons
Substrates

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

New functionalization of myoglobin by chemical modification of heme-propionates. / Hayashi, Takashi; Hisaeda, Yoshio.

In: Accounts of Chemical Research, Vol. 35, No. 1, 31.01.2002, p. 35-43.

Research output: Contribution to journalArticle

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