Xas study of the heme iron coordination in his64(E7)tyr synthetic sperm whale myoglobin

Robert Cortes; Isabella Ascone; Serge Pin; Bernard Alpert; Mark L. Chiu; Stephen G. Sligar

doi:10.7567/JJAPS.32S2.544

Xas study of the heme iron coordination in his64(E7)tyr synthetic sperm whale myoglobin

Robert Cortes
, Isabella Ascone
, Serge Pin
, Bernard Alpert
, Mark L. Chiu
, Stephen G. Sligar

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

Abstract

By using site-directed mutagenesis of the synthetic sperm whale myoglobin, th< native distal histidine residue, at position 64 (the helical position E7), was substituted with; tyrosine. The heme iron coordination in wild-type myoglobin and in His(E7)Tyr mutant wa studied by X-ray Absorption Spectroscopy (XANES and EXAFS). Data show that the iron is bound to the OH group of tvrosine.

Original language	English (US)
Pages (from-to)	544-546
Number of pages	3
Journal	Japanese Journal of Applied Physics
Volume	32
DOIs	https://doi.org/10.7567/JJAPS.32S2.544
State	Published - Jan 1993

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General Engineering
General Physics and Astronomy

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abstract = "By using site-directed mutagenesis of the synthetic sperm whale myoglobin, th< native distal histidine residue, at position 64 (the helical position E7), was substituted with; tyrosine. The heme iron coordination in wild-type myoglobin and in His(E7)Tyr mutant wa studied by X-ray Absorption Spectroscopy (XANES and EXAFS). Data show that the iron is bound to the OH group of tvrosine.",

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year = "1993",

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AU - Cortes, Robert

AU - Ascone, Isabella

AU - Pin, Serge

AU - Alpert, Bernard

AU - Chiu, Mark L.

AU - Sligar, Stephen G.

PY - 1993/1

Y1 - 1993/1

N2 - By using site-directed mutagenesis of the synthetic sperm whale myoglobin, th< native distal histidine residue, at position 64 (the helical position E7), was substituted with; tyrosine. The heme iron coordination in wild-type myoglobin and in His(E7)Tyr mutant wa studied by X-ray Absorption Spectroscopy (XANES and EXAFS). Data show that the iron is bound to the OH group of tvrosine.

AB - By using site-directed mutagenesis of the synthetic sperm whale myoglobin, th< native distal histidine residue, at position 64 (the helical position E7), was substituted with; tyrosine. The heme iron coordination in wild-type myoglobin and in His(E7)Tyr mutant wa studied by X-ray Absorption Spectroscopy (XANES and EXAFS). Data show that the iron is bound to the OH group of tvrosine.

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ER -

Xas study of the heme iron coordination in his64(E7)tyr synthetic sperm whale myoglobin

Abstract

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