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Biochemistry generally focuses on reactions and interactions of biological and organic molecules.
Defination-inorganic biochemistry
The branch of biochemistry concerned with the role of inorganic substances in biochemical systems
metalloproteins
A protein containing a metal ion bound is called metalloprotein Many metalloproteins catalyze important cellular reactions and are thus more specifically called metalloenzymes the metal center can serve as a Lewis acidic site to activate substrates for nucleophilic displacement reactions (that is, hydrolysis).
Proteins fold to form their functional form by bonding with metal ion. Eg hemoglobin
Coor i
ond
Th l ctronic structur of coordination compl x can descri ed in terms of the set of ligands each donating a pair of electrons to a metal centre.
Metal ions have a few characteristics that increase chemical activity: positive charge ability to form strong bonds that are kinetically favored and in some cases their ability to be stable in multiple oxidation states.
Example
Carbonic anhydrase was the first known enzyme to contain zinc
Carbonic anhydrase carries out interconversion of carbondioxide and water to bicarbonate and proton. The reaction catalyzed by carbonic anhydrase is:
Metal-activated enzymes
absolute requirement for the metal ion Phosphofructokinase is an example of a metalactivated enzyme, which catalyzes the reaction
fructose-1,6-
A divalent metal ion (Mg 2+ ) is needed to coordinate the phosphate groups on the ATP molecule in order for phosphofructokinase to successfully catalyze this reaction
metal ions are normally incorporated into the enzymes during enzyme synthesis For example, horse liver alcohol dehydrogenase contains two tightly bound zinc ions . The first zinc ion is structural: bound to four cysteine side chains essential to maintain the structural integrity The second zinc ion is catalytic: bound to the side chains belonging to two cysteines and one histidine at the active site of the enzyme, participates in the catalytic cycle of the enzyme.