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Hydrogenases
The reaction takes place at a specialized metal center that dramatically increases the acidity
of H2 and leads to a heterolytic splitting of the molecule which is strongly accelerated by the …
of H2 and leads to a heterolytic splitting of the molecule which is strongly accelerated by the …
[HTML][HTML] Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers
Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …
photosynthesis and respiration, which are two essential energy processes that sustain all life …
Radical S-Adenosylmethionine Enzymes
JB Broderick, BR Duffus, KS Duschene… - Chemical …, 2014 - ACS Publications
It was once widely held that nearly all reactions in biology were catalyzed via mechanisms
involving paired electron species. Beginning approximately 40 years ago, this paradigm was …
involving paired electron species. Beginning approximately 40 years ago, this paradigm was …
The role of the metal-bound N–H functionality in Noyori-type molecular catalysts
PA Dub, JC Gordon - Nature Reviews Chemistry, 2018 - nature.com
Noyori-type catalysts have found numerous applications in research and industrial settings.
The central mechanistic component of such catalysts is a metal centre coordinated to a N–H …
The central mechanistic component of such catalysts is a metal centre coordinated to a N–H …
[FeFe]-and [NiFe]-hydrogenase diversity, mechanism, and maturation
Abstract The [FeFe]-and [NiFe]-hydrogenases catalyze the formal interconversion between
hydrogen and protons and electrons, possess characteristic non-protein ligands at their …
hydrogen and protons and electrons, possess characteristic non-protein ligands at their …
[HTML][HTML] Protein stability: a crystallographer's perspective
Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …
industries, in addition to being a daily consideration for academic researchers studying …
Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase
T Spatzal, KA Perez, O Einsle, JB Howard, DC Rees - Science, 2014 - science.org
The mechanism of nitrogenase remains enigmatic, with a major unresolved issue
concerning how inhibitors and substrates bind to the active site. We report a crystal structure …
concerning how inhibitors and substrates bind to the active site. We report a crystal structure …
Mimicking hydrogenases: From biomimetics to artificial enzymes
TR Simmons, G Berggren, M Bacchi… - Coordination chemistry …, 2014 - Elsevier
Over the last 15 years, a plethora of research has provided major insights into the structure
and function of hydrogenase enzymes. This has led to the important development of …
and function of hydrogenase enzymes. This has led to the important development of …
Causes and effects of N-terminal codon bias in bacterial genes
Most amino acids are encoded by multiple codons, and codon choice has strong effects on
protein expression. Rare codons are enriched at the N terminus of genes in most organisms …
protein expression. Rare codons are enriched at the N terminus of genes in most organisms …
Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic
J Esselborn, C Lambertz… - Nature chemical …, 2013 - nature.com
Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-
hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose …
hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose …