Crystallographic and FTIR Spectroscopic Evidence of Changes in Fe Coordination Upon Reduction of the Active Site of the Fe-Only Hydrogenase fromDesulfovibriodesulfuricans

2001 ◽  
Vol 123 (8) ◽  
pp. 1596-1601 ◽  
Author(s):  
Yvain Nicolet ◽  
Antonio L. de Lacey ◽  
Xavier Vernède ◽  
Victor M. Fernandez ◽  
E. Claude Hatchikian ◽  
...  
Keyword(s):  
Active Site ◽  
Spectroscopic Evidence

scholarly journals Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase

2020 ◽  
Vol 56 (68) ◽  
pp. 9850-9853
Author(s):  
Ahmed Djeghader ◽  
Melanie Rossotti ◽  
Saleh Abdulkarim ◽  
Frédéric Biaso ◽  
Guillaume Gerbaud ◽  
...  
Keyword(s):  
Active Site ◽  
Spectroscopic Evidence ◽  
Reaction Intermediate

We provide structural and spectroscopic evidence for a molybdenum–phosphate adduct mimicking a proposed reaction intermediate in the active site of a prokaryotic sulfite oxidizing enzyme.

Kinetic and Spectroscopic Evidence for Active Site Inhibition of Human Aldose Reductase†,‡

Biochemistry ◽  
1996 ◽  
Vol 35 (34) ◽  
pp. 11196-11202 ◽  
Author(s):  
Takayuki Nakano ◽  
J. Mark Petrash
Keyword(s):  
Aldose Reductase ◽  
Active Site ◽  
Spectroscopic Evidence

Spectroscopic Evidence of Reversible Disassembly of the [FeFe] Hydrogenase Active Site

2017 ◽  
Vol 8 (16) ◽  
pp. 3834-3839 ◽  
Author(s):  
Patricia Rodríguez-Maciá ◽  
Edward Reijerse ◽  
Wolfgang Lubitz ◽  
James A. Birrell ◽  
Olaf Rüdiger
Keyword(s):  
Active Site ◽  
Spectroscopic Evidence

An Inner-/Outer-Sphere Stabilized Sn Active Site in β-Zeolite: Spectroscopic Evidence and Kinetic Consequences

ACS Catalysis ◽  
2015 ◽  
Vol 6 (1) ◽  
pp. 31-46 ◽  
Author(s):  
Jan Dijkmans ◽  
Michiel Dusselier ◽  
Wout Janssens ◽  
Maarten Trekels ◽  
André Vantomme ◽  
...  
Keyword(s):  
Active Site ◽  
Outer Sphere ◽  
Spectroscopic Evidence ◽  
Β Zeolite

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.

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