Lecture 5

Some ligands can form multiple bonds

transitional metals form complexes with molecules or ions

Measures total protein by reacting with peptide bonds most common automated method

how much a liquid bends light Dissolved substances change refractive index

Globular (soluble) protein Found in red blood cells

Contains heme prosthetic groups Each hemoglobin four heme sites to bind O2 Also participates in CO2 transport

Fe2+ -> Fe3+ when O2 binds

something extra that is added to a protein that is necessary for its functionality Heme is an example

Oxidized form of hemoglobin Fe2+ -> Fe3+ has occurred without binding O2

High levels of methemoglobin Blood turns bluish-brown Treated with methylene blue therapy

Methemoglobin can react with CN- to form a very stable compound Cyanmethemoglobin used to analyze the hemoglobin content of blood

Hemoglobin has much higher affinity for carbon monoxide (CO) than it has for O2 HbO2 + CO -> Hb-CO + O2

high [O2] shifts reaction towards HbO2 low [O2] shifts reaction towards Hb + O2

O2 affinity decreases with increasing CO2 high CO2 triggers the release of bound O2 It is as if hemoglobin “feels” that it should release the O2 when it reaches the cells that need it the most

O2 removal enhances hemoglobin’s affinity for CO2

120 days

Bilirubin

Amino Acids

A1 (A), A2, F (Fetal)

A1

phased out with growth Fetus -> babies -> adults (less 1 %)

mutant forms of hemoglobin produced

low Hb levels caused by bleeding, RBC destruction, or insufficient production as in thalassemia

group of genetic diseases with insufficient production of particular (, , ) globin chains