2 Abstracts Journal of Inorganic Biochemistry

PL01 Proteins and metals, their functional and structural interaction in metalloproteins Robert Huber, Max Planck Institut fur Biochemie,

82152 Martinsried/Germany

Metals and metal-containing cofactors may convey unique catalytic

and redox properties to proteins. Protein metal coordination on the

other hand is often unique generating unusual structures and

electronic states of the metals. This functional and structural

interplay makes metalloproteins a fascinating subject to study.

Metalloprotein structures will be presented in this lecture to

illustrate various aspects of metal protein interaction.

I. Ca may stabilize proteins and mediate protein membrane

interaction; 2. Mg stabilizes cofactor conformations and influences their redox

properties; 3. Zn may polarize ligands in hydrolases; 4. The transition metals V, Fe, Cu are redox active elements in

peroxidases, oxidases and electron carrier proteins; Cu and Fe are able to form multinuclear complexes;

5. Mo uniquely catalyses oxo (i.e.2e transfer processes) in oxidases.

I. -Huber, R. and Bode, W.: Structural Basis of the Activation and Action of Trypsin. (1978) In: Accounts of Chemical Research ii, 114-122.

-Demange, P.et al.:Annexin V:The key to understanding ion selectivity and voltage regulation? (1994) TIBS /~, 272-276.

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

-Bossemeyer, D. et al.: Phosphotransferase and substrate binding mechanism of the cAMP-

dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0~ structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI (5-

24). (1993) The EMBO Journal /~, 849-859. 3. -Bode, W. et al.: The X-ray crystal structure of the catalytic dom, ain of human neutrophil

collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. (1994) The EMBO Journal 13, 1263-1269.

-Gomis-R~th, F.X. et al.: The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C. (1995) The EMBO J./~, 4387-4394.

4. -Messerschmidt, A. and Wever,R.: X-ray structure of a vanadium-containing enzyme: Chloroperoxidase from fungus Curvularia inaequalis. (1996) Proc. Natl. Acad. Sci. USA 93,

392-396. -Romero, A. et al. X-ray Analysis and Spectroscopic Characterization of MI21Q Azurin. A

Copper Site Model for Stellacyanin.(1993) J. Mol. Biol. 229, 1007-1021.

-Messerschmidt, A. et al.:X-ray Structures and Mechanistic Implications of Three Functional Derivatives of Ascorbate Oxidase from Zucchini. Reduced, Peroxide and Azide Forms. (1993) J. Mol. Biol. 230, 997-1014.

-Nar,H.et al.:X-ray Crystal Structure of the Two Site-specific Mutants His35Gln and His35Leu of Azurin from Pseudomonas aeruginosa. (1991) J. Mol. Biol. 218, 427-447. -Archer,M.et al.:Crystal Structure of Desulforedoxin from Desulfovibrio gigas determined at 1.8 ~ Resolution: A novel non-heme Iron Protein Structure. (1995) J. Mol. Biol. 251, 690- 702. -Macedo-Ribeiro, S. et al.: Small structural changes account for the high thermostability of l[4Fe-4S]ferrodoxin from the hyperthormophilic bacterium Thermotoga maritima. (1996) Structure ~, 1291-1301.

5. -Huber, R. et al: A Structure-based Catalytic Mechanism for the Xanthine Oxidase Family of Molybdenum Enzymes. (1996) Proc. Natl. Acad, Sci. USA 93, 8846-8851.

-Romao, M.J. et al.: Crystal Structure of the Xanthine Oxidase-related Aldehyde Oxido- Reductase from D. gigas. (1995) SCIENCE 270, 1170-1176.