Assignment(s) Deck Flashcards
In coordination chemistry the donor atom of a ligand is_________
The atom in the ligand that shares an electron pair with the metal
The biological functions of carbonic anhydrase and alcohol dehydrogenase, respectively are________
Interconversion of CO2 and carbonates, and alcohols, and aldehyde
The active sites of carboxypeptidase A contains______ and catalyzes_______
Zn(II); the hydrolysis of peptide bonds
The ligand system found in hemoglobin and myoglobin is ___________
Porphyrin
The binding of O2 to hemoglobin shifts from low affinity to high affinity state as____________
Partial pressure of O2 increases
The amino acid side chains that acts as ligands and with high affinity for Fe3+ in transferrin are __________
Tyrosine, histidine, and aspartate
Ferritins in biological systems are involved in__________
Storage of Fe
Siderophores are small polydentate ligands with high affinity for iron. Their main role is to __________
Aid iron uptake/mobilization
Identify the biological function of hemocyanin and the metal ion responsible for its function.
O2 transport and Cu
Which one of the following is NOT the essential functions of iron in biological systems?
Muscle movement
The amino acid side chains that act as ligands for the binding of Ca2+ in Calmodulin are _____________
Aspartate, glutamate, and peptide carbonyls
Iron-Sulfur clusters in biological systems are involved in __________
Electron transfer
A well-known naturally occurring organometallic compound is___________
Vitamin B12 coenzyme
The main biological function of cytochrome-c peroxidase is _____________
Reduction of H2O2 to water
Identify the biological function of cytochrome-c and the metal responsible for its function.
Electron transfer and Fe