usehemoglobinmyoglobinasanexampleofasolubleprotein.pptVIP

Hemoglobin : a portrait of a soluble protein with 4° stuctureTHE OBJECTIVES Evolution from Anaerobic to Aerobic Life Timeline Universe is 12-20 billion years old Earth is 4.6 billion years old Life began 3.5 billion years ago (Anaerobic) Aerobic Life (Us) began 0.6 billion years ago Iron, Oxygen, and Life Pre-Biotic: little O2, more CH4, H2S, H2 Iron primarily Fe2+ [Fe2+] = 2 x 10-4 M in water Only simple transport of Fe2+ needed Anaerobic Life Simple, 1-celled organisms Don’t use O2 for metabolism Blue-green Algae Develop Photosynthesis O2 produced as biproduct Fe2+ oxidized to Fe3+ [Fe3+] = 10-7 M in water Molecules Evolve to Destroy O2 (catalase) Molecules Evolve to Solubilize and Transport Iron Reduce Fe3+ to Fe2+ Keep iron from oxidizing back to Fe3+ 0.6 Billion Years Ago, [O2] reaches 1% Aerobic Life Evolves Use O2 in Metabolism 18 times as much energy from glucose in the presence of O2 as without it [O2] = 1.2 x 10-3 M in water O2 transport molecules must evolve Oxygen Carrying Molecules Hemorythrin O2 transport protein in certain sea worms Uses a diiron binding site Hemocyanin O2 transport protein in mollusks and arthropods Uses a dicopper binding site Gives them blue blood Myoglobin and Hemoglobin Myoglobin and Hemoglobin are oxygen carrying molecules that overcome the problem that vertebrates have with the low solubility of oxygen in water Oxygen binds to the Heme prosthetic group Myoglobin Heme Prosthetic Group Prosthetic Group = non-polypeptide unit of a protein that can function without the protein Apoprotein = protein without its P.G. Many proteins require a P.G. for activity Protoporphyrin IX + Fe is the Heme P.G. Many “porphyrines” exist in organisms Naturally occurring macrocyclic ligand Ligand = organic molecule which binds a metal ion by donating 2 e- from a donor atom (N:) Macrocycle = ligand with donor atoms arranged in a ring Strongly binds Fe because of rigid macrocyclic structure Fe in the porphyrine makes it a Heme