Hemoglobin Flashcards
final enzyme of electron transport
cytochrome oxidase - O2 is reduced to H2O
facilitates O2 diffusion to the mitochondrion
Mb
function of Mb
intracellular transport and temporary storage of O2 needed for aerobic metabolism of muscle
secondary structure of Mb
8 a-helices
quaternary structure of Hb
a2B2
- 2 x a:B dimers
- quilibrium favors tetramer
ApoHb vs HoloHb
protein without vs with prosthetic group
-HoloHb = 1 heme/subunit = 4 hemes
how many hemes/O2 binding sites in Hb
4 (1/subunit)
basis for Hb’s cooperative binding, resulting in a sigmoid binding curve
T vs R
-R = more O2 bound = higher O2 affinity until Hb molecule is sat’d
porphyrin
- tetrapyrrole
- forms protoporphyrin IX, which chelates Fe
metal chelating site on Hb
- binds Fe
- 4 nitrogens of 4 pyrrole groups point inward
substituent groups on heme prosthetic group (a pyrrole)
4 methyl, 2 vinyl, 2 propionate
state of Fe in deoxyHb
ferrous = Fe(II)
-reduced
(high/low) O2 affinity at P50
high
Mb vs Hb curve
hyperbolic vs sigmoidal
Mb ___ O2 in conditions under which Hb ____ it
binds
releases