Influence of thiolate ligation on the heme electronic structure in microsomal cytochrome P-450 and model compounds: resonance Raman spectroscopic evidence

1989 ◽  
Vol 28 (25) ◽  
pp. 4491-4495 ◽  
Author(s):  
Pavel Anzenbacher ◽  
Ruby Evangelista-Kirkup ◽  
John Schenkman ◽  
Thomas G. Spiro
Keyword(s):  
Electronic Structure ◽  
Resonance Raman ◽  
Model Compounds ◽  
Microsomal Cytochrome ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic ◽  
Heme Electronic Structure ◽  
Cytochrome P 450

Resonance Raman spectroscopic evidence for the formation of covalent complexes between N-acylamino acid dithioesters and mercury papain

1987 ◽  
Vol 65 (7) ◽  
pp. 1521-1526 ◽  
Author(s):  
Ho-Hi Lee ◽  
Ronald H. Angus ◽  
Paul R. Carey ◽  
Andrew C. Storer
Keyword(s):  
Active Site ◽  
Resonance Raman ◽  
Product Formation ◽  
Side Chain ◽  
Model Compounds ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic ◽  
The Difference

Ethyl dithioesters of N-acylglycine and N-acylalanine are shown to bind tightly to the active site of papain in which the side chain of cysteine-25 is in the mercurated form. Although both classes of dithioester bind to the active site mercury via their thiono (C=S) sulfur atoms, the resulting adducts are quite different. Absorption and resonance Raman data, supported by comparison with model compounds and by 15N and 13C=S isotopic substitutions, show that the glycine and alanine dithioesters are converted to enethiolates and 4-methyloxazolin-5-thiones, respectively. The difference in product formation is explained by a mechanism in which stereospecific proton removal is brought about by the -COO− side chain of Asp-158, which is situated in the vicinity of the active site. For glycine dithioesters the Asp-158 catalyses the removal of a Cα proton whereas for alanine dithioesters the alanine's NH proton is removed.

Resonance Raman spectroscopic evidence for a common [3-iron-4-sulfur] structure among proteins containing three-iron centers

1983 ◽  
Vol 105 (22) ◽  
pp. 6671-6678 ◽  
Author(s):  
Michael K. Johnson ◽  
Roman S. Czernuszewicz ◽  
Thomas G. Spiro ◽  
James A. Fee ◽  
William V. Sweeney
Keyword(s):  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic

Electronic and resonance raman spectroscopic evidence for identification of μ-trihalobis(triammine-ruthenium)(2+) ions as delocalized Ru(II,III) mixed-valence complexes

1984 ◽  
Vol 89 (3) ◽  
pp. L33-L34 ◽  
Author(s):  
Robert S. Armstrong ◽  
James K. Beattie ◽  
Patricia Del Favero ◽  
Vivienne M. Ellis ◽  
Noel S. Hush
Keyword(s):  
Mixed Valence ◽  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic

scholarly journals Soluble Guanylate Cyclase Is Activated Differently by Excess NO and by YC-1: Resonance Raman Spectroscopic Evidence

Biochemistry ◽  
2010 ◽  
Vol 49 (23) ◽  
pp. 4864-4871 ◽  
Author(s):  
Mohammed Ibrahim ◽  
Emily R. Derbyshire ◽  
Alexandra V. Soldatova ◽  
Michael A. Marletta ◽  
Thomas G. Spiro
Keyword(s):  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic

Conformational Analysis of Mitochondrial and Microsomal Cytochrome P-450 by Resonance Raman Spectroscopy

Biochemistry ◽  
1994 ◽  
Vol 33 (43) ◽  
pp. 12920-12929 ◽  
Author(s):  
Peter Hildebrandt ◽  
George Heibel ◽  
Pavel Anzenbacher ◽  
Reinhard Lange ◽  
Volker Krueger ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Conformational Analysis ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Microsomal Cytochrome ◽  
Cytochrome P 450
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