A simple yet multifaceted 90 years old, evergreen enzyme: Carbonic anhydrase, its inhibition and activation

CT Supuran - Bioorganic & Medicinal Chemistry Letters, 2023 - Elsevier
Advances in the carbonic anhydrase (CA, EC 4.2. 1.1) research over the last three decades
are presented, with an emphasis on the deciphering of the activation mechanism, the …

Structure and mechanism of carbonic anhydrase

S Lindskog - Pharmacology & therapeutics, 1997 - Elsevier
Carbonic anhydrase (CA; carbonate hydro-lyase, EC 4.2. 1.1) is a zinc-containing enzyme
that catalyzes the reversible hydration of carbon dioxide: CO2+ H2O↔ HCO3−+ H+. The …

Fast CO2 hydration kinetics impair heterogeneous but improve enzymatic CO2 reduction catalysis

SJ Cobb, VM Badiani, AM Dharani, A Wagner… - Nature …, 2022 - nature.com
The performance of heterogeneous catalysts for electrocatalytic CO2 reduction suffers from
unwanted side reactions and kinetic inefficiencies at the required large overpotential …

A proficient enzyme

A Radzicka, R Wolfenden - Science, 1995 - science.org
Orotic acid is decarboxylated with a half-time (t1/2) of 78 million years in neutral aqueous
solution at room temperature, as indicated by reactions in quartz tubes at elevated …

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein− ligand binding

VM Krishnamurthy, GK Kaufman, AR Urbach… - Chemical …, 2008 - ACS Publications
Carbonic anhydrase (CA, EC 4.2. 1.1) is a protein that is especially well-suited to serve as a
model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of …

Prokaryotic carbonic anhydrases

KS Smith, JG Ferry - FEMS microbiology reviews, 2000 - academic.oup.com
Carbonic anhydrases catalyze the reversible hydration of CO2 []. Since the discovery of this
zinc (Zn) metalloenzyme in erythrocytes over 65 years ago, carbonic anhydrase has not only …

Voltage-gated proton channels and other proton transfer pathways

TE Decoursey - Physiological reviews, 2003 - journals.physiology.org
Proton channels exist in a wide variety of membrane proteins where they transport protons
rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules …

The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water

DN Silverman, S Lindskog - Accounts of Chemical Research, 1988 - ACS Publications
C02+ H20^ HC03-+ H+(1) This is a very simple enzymic reactioninvolving only six substrate
atoms and, at least formally, the transfer of an OH™ moiety from H20 to C02. Extensive …

Human sulfide: quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite

MR Jackson, SL Melideo, MS Jorns - Biochemistry, 2012 - ACS Publications
Sulfide: quinone oxidoreductase (SQOR) is a membrane-bound enzyme that catalyzes the
first step in the mitochondrial metabolism of H2S. Human SQOR is successfully expressed at …

Refined structure of human carbonic anhydrase II at 2.0 Å resolution

AE Eriksson, TA Jones, A Liljas - Proteins: Structure, Function …, 1988 - Wiley Online Library
The structure of human erythrocytic carbonic anhydrase II has been refined by constrained
and restrained structure–factor least‐squares refinement at 2.0 Å resolution. The …