Lista de obras - James D. Reid - Dominio Público Uruguay

A classical enzyme active center motif lacks catalytic competence until modulated electrostatically

scientific article published on 01 August 1997

Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex

artículo científico publicado en 2001

Characterization of the magnesium chelatase from Thermosynechococcus elongatus.

artículo científico publicado en 2014

Direct measurement of metal-ion chelation in the active site of the AAA+ ATPase magnesium chelatase

artículo científico publicado en 2007

Five glutamic acid residues in the C-terminal domain of the ChlD subunit play a major role in conferring Mg(2+) cooperativity upon magnesium chelatase

artículo científico publicado en 2015

Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation.

artículo científico publicado en 2004

Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.

artículo científico publicado en 2004

Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase

artículo científico publicado en 2009

Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation

artículo científico publicado en 2000

Nonequilibrium Isotope Exchange Reveals a Catalytically Significant Enzyme–Phosphate Complex in the ATP Hydrolysis Pathway of the AAA+ ATPase Magnesium Chelatase ⬇️

artículo científico publicado el 29 de febrero de 2012

Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803

artículo científico publicado en 2003

Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis

artículo científico publicado en 2005

The ATPase activity of the ChlI subunit of magnesium chelatase and formation of a heptameric AAA+ ring.

artículo científico publicado en 2003

The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase

artículo científico publicado en 2019

The active site of magnesium chelatase

artículo científico publicado en 2020

The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.

artículo científico publicado en 2013

Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.

artículo científico publicado en 2003

Lista de obras de James D. Reid

A classical enzyme active center motif lacks catalytic competence until modulated electrostatically

Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex

Characterization of the magnesium chelatase from Thermosynechococcus elongatus.

Direct measurement of metal-ion chelation in the active site of the AAA+ ATPase magnesium chelatase

Five glutamic acid residues in the C-terminal domain of the ChlD subunit play a major role in conferring Mg(2+) cooperativity upon magnesium chelatase

Isomerization of the uncomplexed actinidin molecule: kinetic accessibility of additional steps in enzyme catalysis provided by solvent perturbation.

Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.

Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase

Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation

Nonequilibrium Isotope Exchange Reveals a Catalytically Significant Enzyme–Phosphate Complex in the ATP Hydrolysis Pathway of the AAA+ ATPase Magnesium Chelatase ⬇️

Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803

Structural and biochemical characterization of Gun4 suggests a mechanism for its role in chlorophyll biosynthesis

The ATPase activity of the ChlI subunit of magnesium chelatase and formation of a heptameric AAA+ ring.

The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase

The active site of magnesium chelatase

The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.

Variation in the pH-dependent pre-steady-state and steady-state kinetic characteristics of cysteine-proteinase mechanism: evidence for electrostatic modulation of catalytic-site function by the neighbouring carboxylate anion.