Nonredox nickel enzymes
MJ Maroney, S Ciurli - Chemical reviews, 2014 - ACS Publications
The importance of nickel enzymes, where nickel serves as an essential cofactor, in Archaea,
bacteria, plants, and primitive eukaryotes, is well documented. 1 Despite the fact that no …
bacteria, plants, and primitive eukaryotes, is well documented. 1 Despite the fact that no …
Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies
JA Gerlt, PC Babbitt - Annual review of biochemistry, 2001 - annualreviews.org
▪ Abstract The protein sequence and structure databases are now sufficiently representative
that strategies nature uses to evolve new catalytic functions can be identified. Groups of …
that strategies nature uses to evolve new catalytic functions can be identified. Groups of …
A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels
Background: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen
mineralization, using a bimetallic nickel centre. The role of the active site metal ions and …
mineralization, using a bimetallic nickel centre. The role of the active site metal ions and …
The catalytic mechanisms of binuclear metallohydrolases
Binuclear metallohydrolases are a structurally diverse group of enzymes that use binuclear
metal ion centers to catalyze the hydrolysis of amides and esters of carboxylic and …
metal ion centers to catalyze the hydrolysis of amides and esters of carboxylic and …
Interplay of metal ions and urease
EL Carter, N Flugga, JL Boer, SB Mulrooney… - Metallomics, 2009 - academic.oup.com
Urease, the first enzyme to be crystallized, contains a dinuclear nickel metallocenter that
catalyzes the decomposition of urea to produce ammonia, a reaction of great agricultural …
catalyzes the decomposition of urea to produce ammonia, a reaction of great agricultural …
Structures of Cys319 Variants and Acetohydroxamate-Inhibited Klebsiella aerogenes Urease,
Cys319 is located on a mobile flap covering the active site of Klebsiella aerogenes urease
but does not play an essential role in catalysis. Four urease variants altered at position C319 …
but does not play an essential role in catalysis. Four urease variants altered at position C319 …
Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms
This work provides a comprehensive critical summary of urease spectroscopy,
crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis …
crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis …
Active sites of transition-metal enzymes with a focus on nickel
U Ermler, W Grabarse, S Shima, M Goubeaud… - Current opinion in …, 1998 - Elsevier
Since 1995, crystal structures have been determined for many transition-metal enzymes, in
particular those containing the rarely used transition metals vanadium, molybdenum …
particular those containing the rarely used transition metals vanadium, molybdenum …
The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65-Å resolution
The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly
ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic …
ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic …
Nickel complexes of carboxylate-containing polydentate ligands as models for the active site of urease
H Carlsson, M Haukka, A Bousseksou… - Inorganic …, 2004 - ACS Publications
Two new carboxylate-containing polydentate ligands have been synthesized, the symmetric
ligand 2, 6-bis [N-(N-(carboxylmethyl)-N-((1-methylimidazol) methyl) amine) methyl]-4 …
ligand 2, 6-bis [N-(N-(carboxylmethyl)-N-((1-methylimidazol) methyl) amine) methyl]-4 …