Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal

S Della Longa; Alessandro Arcovito; M Girasole; Jl Hazemann; M. Benfatto

Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal

S Della Longa, Alessandro Arcovito, M Girasole, Jl Hazemann, M. Benfatto

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

Abstract

We report the first quantitative analysis of the Fe K-edge polarized x-ray absorption near edge structure of the iron protein carbonmonoxy-myoglobin (MbCO) single crystal and of its cryogenic photoproduct Mb(*)CO. The CO-Fe-heme local structure has been determined using a novel fitting procedure based on the full multiple scattering approach. The extracted local structure of Mb(*)CO includes a Fe-CO distance of (3.08+/-0.07) A, with a tilting angle between the heme normal and the Fe-C vector of (37+/-7) degrees, and a bending angle between the Fe-C vector and the C-O bond of (31+/-5) degrees.

Original language	English
Pages (from-to)	155501-155501
Number of pages	1
Journal	Physical Review Letters
Volume	87
Publication status	Published - 2001

Keywords

Animals
Binding Sites
Carbon Monoxide
Crystallography, X-Ray
Heme
Iron
Myoglobin
Photolysis
Protein Conformation
Scattering, Radiation
Spectrometry, X-Ray Emission
Whales

Cite this

@article{a6ba0681954b4fb29a75288a15091274,

title = "Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal",

abstract = "We report the first quantitative analysis of the Fe K-edge polarized x-ray absorption near edge structure of the iron protein carbonmonoxy-myoglobin (MbCO) single crystal and of its cryogenic photoproduct Mb(*)CO. The CO-Fe-heme local structure has been determined using a novel fitting procedure based on the full multiple scattering approach. The extracted local structure of Mb(*)CO includes a Fe-CO distance of (3.08+/-0.07) A, with a tilting angle between the heme normal and the Fe-C vector of (37+/-7) degrees, and a bending angle between the Fe-C vector and the C-O bond of (31+/-5) degrees.",

keywords = "Animals, Binding Sites, Carbon Monoxide, Crystallography, X-Ray, Heme, Iron, Myoglobin, Photolysis, Protein Conformation, Scattering, Radiation, Spectrometry, X-Ray Emission, Whales, Animals, Binding Sites, Carbon Monoxide, Crystallography, X-Ray, Heme, Iron, Myoglobin, Photolysis, Protein Conformation, Scattering, Radiation, Spectrometry, X-Ray Emission, Whales",

author = "{Della Longa}, S and Alessandro Arcovito and M Girasole and Jl Hazemann and M. Benfatto",

year = "2001",

language = "English",

volume = "87",

pages = "155501--155501",

journal = "Physical Review Letters",

issn = "0031-9007",

publisher = "American Institute of Physics:2 Huntington Quadrangle, Suite 1NO1:Melville, NY 11747:(800)344-6902, (631)576-2287, EMAIL: [email protected], INTERNET: http://www.aip.org, Fax: (516)349-9704",

}

TY - JOUR

T1 - Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal

AU - Della Longa, S

AU - Arcovito, Alessandro

AU - Girasole, M

AU - Hazemann, Jl

AU - Benfatto, M.

PY - 2001

Y1 - 2001

N2 - We report the first quantitative analysis of the Fe K-edge polarized x-ray absorption near edge structure of the iron protein carbonmonoxy-myoglobin (MbCO) single crystal and of its cryogenic photoproduct Mb(*)CO. The CO-Fe-heme local structure has been determined using a novel fitting procedure based on the full multiple scattering approach. The extracted local structure of Mb(*)CO includes a Fe-CO distance of (3.08+/-0.07) A, with a tilting angle between the heme normal and the Fe-C vector of (37+/-7) degrees, and a bending angle between the Fe-C vector and the C-O bond of (31+/-5) degrees.

AB - We report the first quantitative analysis of the Fe K-edge polarized x-ray absorption near edge structure of the iron protein carbonmonoxy-myoglobin (MbCO) single crystal and of its cryogenic photoproduct Mb(*)CO. The CO-Fe-heme local structure has been determined using a novel fitting procedure based on the full multiple scattering approach. The extracted local structure of Mb(*)CO includes a Fe-CO distance of (3.08+/-0.07) A, with a tilting angle between the heme normal and the Fe-C vector of (37+/-7) degrees, and a bending angle between the Fe-C vector and the C-O bond of (31+/-5) degrees.

KW - Animals

KW - Binding Sites

KW - Carbon Monoxide

KW - Crystallography, X-Ray

KW - Heme

KW - Iron

KW - Myoglobin

KW - Photolysis

KW - Protein Conformation

KW - Scattering, Radiation

KW - Spectrometry, X-Ray Emission

KW - Whales

KW - Animals

KW - Binding Sites

KW - Carbon Monoxide

KW - Crystallography, X-Ray

KW - Heme

KW - Iron

KW - Myoglobin

KW - Photolysis

KW - Protein Conformation

KW - Scattering, Radiation

KW - Spectrometry, X-Ray Emission

KW - Whales

UR - http://hdl.handle.net/10807/11814

M3 - Article

SN - 0031-9007

VL - 87

SP - 155501

EP - 155501

JO - Physical Review Letters

JF - Physical Review Letters

ER -

Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal

Abstract

Keywords

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