PROTEINS – CLASSES AND FUNCTIONS

dynamic

catalysis enzymes
transport hemoglobin
protection antibodies
muscle contraction actin and myosin
metabolic control hormones
gene transcription histones
storage ferritin

structural

matrices for bone collagen and elastin

and connective tissue
 PROTEINS

apoprotein – amino acids only

cofactors – small organic (e.g., vitamins, ATP, NAD, FAD) or

inorganic (metal ions) units that are required for activity; can be
loosely bound (coenzymes) or tightly bound (prosthetic groups)

prosthetic group – tightly bound group (e.g., heme) to apoprotein

holoprotein – active protein with cofactors and prosthetic groups

attached
 COFACTORS

Participate directly in catalytic processes; binding to proteins may

be weak or strong

Required in small quantities

functions

1.metal ions maintain protein conformation through

electrostatic interactions
2. prosthetic groups like heme may bind to active site and change

the conformation
3. may accept a substrate during reaction
 METAL ION LIGATION

Metal ions are bound in mononuclear or polynuclear coordination

units in which amino acid side chains function as endogenous
chelating ligands

Quite often protein ligation does not coordinately saturate metal ion
coordination environments – catalysis

common bridging ligands

O2-, OH-, -CH2S-, S2-, -CH2CO2-, imidazole

exogenous terminal ligands are also often bound to metal ions

H2O, OH-, O2-, HS-, S2-
 ENDOGENOUS METAL ION
LIGATION Protein residues as ligands for metal ions

Oxygen atoms of peptide carbonyls, nitrogen atoms of deprotonated

backbone amides, and lysine side chains are also available for metal
coordination. 5
ENDOGENOUS METAL ION
LIGATION
ENDOGENOUS METAL ION
LIGATION