Dieter v. Ehrenstein

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Ligand binding to heme proteins is studied by using flash photolysis over wide ranges in time (100 ns-1 ks) and temperature (10-320 K). Below about 200 K in 75% glycerol/water solvent, ligand rebinding occurs from the heme pocket and is nonexponential in time. The kinetics is explained by a distribution, g(H), of the enthalpic barrier of height H between(More)
Azurin is a small blue copper protein in the electron transfer chain of denitrifying bacteria. It forms a photolabile complex with nitric oxide (NO) at low temperatures. We studied the temperature dependence of the ligand binding equilibrium and the kinetics of the association reaction after photodissociation over a wide range of temperature (80-280 K) and(More)
Type 1 copper sites bind nitric oxide (NO) in a photolabile complex. We have studied the NO binding properties of the type 1 copper sites in two cupredoxins, azurin and halocyanin, by measuring the temperature dependence of the ligand binding equilibria and the kinetics of the association reaction after photodissociation over a wide range of temperature(More)
Auf l6sungsverm6gen un te r t 00000 ver langt . Hier ist der m i t dem F P S p e k t r o m e t e r erziel te L ich tgewinn besonders wesent l ich , da im U l t r a r o t e n noch n ich t Empf / inger m i t der gleichen h o h e n Empf ind l i chke i t , wie sie Mult ipl ier im S ich tba ren besi tzen, zur Verf i igung s tehen . I m Gegensa tz zu der A n w e(More)
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