Deisenhofer

Deisenhofer J, Epp O, Miki K, Huber R and Michei H 1984 X-ray structure anaiysis of a membrane-protein compiex eiectron density map at 3 A resoiution and a modei of the chromophores of the photosynthetic reaction center from Rhode pseudomonas viridis J. Mol. Biol. 180 385-98... 

Wlodawer, A., Deisenhofer, J., Huber, R. Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor. /. Mol. Biol. 193 145-156, 1987. 

Kobe, B., Deisenhofer, J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 366 751-756, 1993. 

Deisenhofer, J., Michael, H. Nobel lecture. The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis. EMBO f. 8 2149-2169, 1989. 

Michel, H., Deisenhofer, J. Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II. BicKhemistry 27 1-7, 1988. 

Deisenhofer, J., et al. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A resolution. Nature 318 618-624, 1985. 

Deisenhofer, J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 A resolution. Biochemistry 20 2361-2369, 1981. 

The structure of the UQ-cyt c reductase, also known as the cytochrome bc complex, has been determined by Johann Deisenhofer and his colleagues. (Deisenhofer was a co-recipient of the Nobel Prize in Chemistry for his work on the structure of a photosynthetic reaction center [see Chapter 22]). The complex is a dimer, with each monomer consisting of 11 protein subunits and 2165 amino acid residues (monomer mass, 248 kD). The dimeric structure is pear-shaped and consists of a large domain that extends 75 A into the mito-... 

What molecular architecture couples the absorption of light energy to rapid electron-transfer events, in turn coupling these e transfers to proton translocations so that ATP synthesis is possible Part of the answer to this question lies in the membrane-associated nature of the photosystems. Membrane proteins have been difficult to study due to their insolubility in the usual aqueous solvents employed in protein biochemistry. A major breakthrough occurred in 1984 when Johann Deisenhofer, Hartmut Michel, and Robert Huber reported the first X-ray crystallographic analysis of a membrane protein. To the great benefit of photosynthesis research, this protein was the reaction center from the photosynthetic purple bacterium Rhodopseudomonas viridis. This research earned these three scientists the 1984 Nobel Prize in chemistry. 

FIGURE 22.17 The R. viridis reaction center is coupled to the cytochrome h/Cl complex through the quinone pool (Q). Quinone molecules are photore-duced at the reaction center Qb site (2 e [2 hv] per Q reduced) and then diffuse to the cytochrome h/ci complex, where they are reoxidized. Note that e flow from cytochrome h/ci back to the reaction center occurs via the periplasmic protein cytochrome co- Note also that 3 to 4 are translocated into the periplasmic space for each Q molecule oxidized at cytochrome h/ci. The resultant proton-motive force drives ATP synthesis by the bacterial FiFo ATP synthase. (Adapted from Deisenhofer, and Michel, H., 1989. The photosynthetic reaction center from the purple bac-terinm Rhod.opseud.omoaas viridis. Science 245 1463.)... 

Deisenhofer, J., and Michel, H., 1989. The photosyndietic reaction center from die purple bacterium Rhodopseudomonas viridis. Science 245 1463-1473. Published version of die Nobel laureate address by the researchers who first elucidated the molecnlar structure of a photosyndietic reacdon center. 

Deisenhofer,/, Michel, H., and Huber, R., 1985. The structural basis of light reacdons in bacteria. Trends in Biochemical Sciences 10 243-248. 

Zhang H, Seabra MC, Deisenhofer J (2000) Crystal structure of Rab geranylgeranyltransferase at 2.0 angsttom resolution. Structure Fold Des 8(3) 241-251... 

Rieger B, Deisenhofer S, Feifel T, Kukral J, Klinga M, Leskela M (2003) Asymmetric metallocene catalysts based on dibenzothiophene a new approach to high molecular weight polypropylene plastomers. Organometallics 22 3495-3501... 

Rieger B, Troll C, Hild S, Cobzaru C, Deisenhofer S, Hearley A (2005) Novel high and ult-rahigh molecular weight poly(propylene) plastomers by asymmetric hafnocene catalysts. Macromol Chem Phys 206 1231-1240... 

Deisenhofer S (2002) Entwicklung neuer Zirkonocen- und Hafnocen-Katalysatorarchitekturen und deren Verwendung in der metallocenkatalysierten Olefinpolymerisation. Dissertation, Ulm... 

HASEMANN, C.A., KURUMBAIL R.G., BODDUPALLI, S.S., PETERSON, J.A., DEISENHOFER, J., Structure and function of cytochromes P450 A comparative analysis of three crystal structures, Structure, 1995, 3,41-62. 

Another computational approach for detecting /1-solenoid sequences is implemented in a program called BETAWRAP (Bradley et al., 2001). This approach aims to identify /1-solenoid sequences by using hydrophobic-residue sequence patterns of strand-turn-strand regions that were learned from non-/l-solenoid structures. This method also takes into consideration the repetitive character of these patterns in /1-solenoids. Unlike the sequence profile approaches, BETAWRAP can make ab initio predictions of /1-solenoid domains. However, it is less sensitive than the profile search and, sometimes, cannot distinguish /1-solenoids from other solenoids (A. V. K, unpublished observation) such as, for example, LRR proteins (Kobe and Deisenhofer, 1994 Kobe and Kajava, 2001). The latest modification of BETAWRAP algorithm, which is called BETAWRAPPRO (McDonnell et al., 2006), employs additional data provided by sequence profiles and this improves the results of /1-solenoid predictions. 

Kobe, B., and Deisenhofer, J. (1994). The leucine-rich repeat A versatile binding motif. 

Xia, D., Henry, L.J., Gerard, R. D., and Deisenhofer, J. (1994). Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution. Structure 2, 1259-1270. 

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