Aconitase as iron-sulfur protein, enzyme, and iron-regulatory protein

Article Abstract:

Aconitase is an iron-sulfur (Fe-S) protein with enzymatic properties that acts as an iron-regulatory protein for intracellular iron homeostasis. The 4Fe-4S cluster is sterically free to interact with the substrates to form chelates with carboxyl and hydroxyl groups. The Fe4 site in aconitase functions in enzyme catalysis by delocalizing the electron density in the transition state and reducing the pK(sub a) of a water molecule bound to the metal. The mitochondrial, plant and bacterial aconitase show sequence similarity with an iron regulatory protein.

Observations, Proteins, Iron, Iron (Metal), Amino acid sequence, Amino acid sequencing

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Artificial enzymes

Article Abstract:

Artificial enzymes are modified proteins which function as enzymatic catalysts in different reactions. Holoenzymes requiring coenzyme factors such as vitamin B1, B2, B6, and B12 catalyze various biological reactions such as beta-replacement reactions, transamination reactions, and nonoxidative decarboxylation. Artificial enzymes including heme and NADH participate in a series of redox reactions of the biological systems. Vitamin B12 is important for turnover and enantioselective reactions.

Analysis, Chemical reactions, NAD (Coenzyme), Vitamin B complex, Nicotinamide adenine dinucleotide

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Magnetic field effects in biology: a survey of possible mechanisms with emphasis on radical-pair recombination

Article Abstract:

various plausible mechanisms help explain the possible biological effects of static and time-varying magnetic fields. One of the mechanisms involves the formation of radical pair (RP) intermediates. The influence of magnetic field effects on radical pair recombination is discussed. RP intermediates associated with the photosynthetic reaction and enzymes are examined. Mechanism which do not involve changes in RP recombination are analyzed.

Physiological aspects, Magnetic fields

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