The catalytic copper of peptidylglycine α-hydroxylating monooxygenase also plays a critical structural role

Biophysical Journal

Volumn 89, Issue 5, 2005, Pages 3312-3319

  Siebert, Xavier ^a   Eipper, Betty A ^b   Mains, Richard E ^b   Prigge, Sean T ^c   Blackburn, Ninian J ^d   Amzel, L Mario ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

^c JOHNS HOPKINS BLOOMBERG SCHOOL OF PUBLIC HEALTH   (United States)

^d OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE; ISOLEUCINE; LIGAND; METHIONINE; MUTANT PROTEIN; PEPTIDYLGLYCINE ALPHA HYDROXYLATING MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

AMIDATION; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTALLIZATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME STABILITY; ENZYME STRUCTURE; EXTENDED X RAY ABSORPTION FINE SPECTROSCOPY; MUTATION; OXIDATION; ROENTGEN SPECTROSCOPY; STRUCTURE ANALYSIS;

EID: 27744459340     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.066100     Document Type: Article

References (34)

1. Cuttitta, F. 1993. Peptide amidation: signature of bioactivity. Anat. Rec. 236:87-93.
2. Eipper, B. A., D. A. Stoffers, and R. E. Mains. 1992. The biosynthesis of neuropeptides: peptide α-amidation. Annu. Rev. Neurosci. 15:57-85.
3. Merkler, D. J. 1994. C-terminal amidated peptides: production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity. Enzyme Microb. Technol. 16: 450-456.
4. Bradbury, A. F., M. D. Finnie, and D. G. Smyth. 1982. Mechanism of C-terminal amide formation by pituitary enzymes. Nature. 298:686-688.
5. Prigge, S. T., A. S. Kolhekar, B. A. Eipper, R. E. Mains, and L. M. Amzel. 1997. Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase. Science. 278: 1300-1305.
6. Prigge, S. T., A. S. Kolhekar, B. A. Eipper, R. E. Mains, and L. M. Amzel. 1999. Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase. Nat. Struct. Biol. 6:976-983.
7. Eipper, B. A., A. S. Quon, R. E. Mains, J. S. Boswell, and N. J. Blackburn. 1995. The catalytic core of peptidylglycine alpha-hydroxylating monooxygenase: investigation by site-directed mutagenesis, Cu x-ray absorption spectroscopy, and electron paramagnetic resonance. Biochemistry. 34:2857-2865.
8. Jaron, S., R. E. Mains, B. A. Eipper, and N. J. Blackburn. 2002. The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant. Biochemistry. 41:13274-13282.
9. Freeman, J. C., J. J. Villafranca, and D. J. Merkler. 1993. Redox cycling of enzyme-bound copper during peptide amidation. J. Am. Chem. Soc. 115:4923-4924.
10. Bell, J., R. El Meskini, D. D'Amato, R. E. Mains, and B. A. Eipper. 2003. Mechanistic investigation of peptidylglycine alpha-hydroxylating Monooxygenase vias intrinsic tryptophan fluorescence and mutagenesis. Biochemistry. 42:7133-7142.
11. Francisco, W. A., D. J. Merkler, N. J. Blackburn, and J. P. Klinrnan. 1998. Kinetic mechanism and intrinsic isotope effects for the peptidylglycine alpha-amidating enzyme reaction. Biochemistry. 37:8244-8252.
12. Kulathila, R., A. P. Consalvo, P. F. Fitzpatrick, J. C. Freeman, L. M. Snyder, J. J. Villafranca, and D. J. Merkler. 1994. Bifunctional peptidylglcine alpha-amidating enzyme requires two copper atoms for maximum activity. Arch. Biochem. Biophys. 311:191-195.
13. Kolhekar, A. S., H. T. Keutmann, R. E. Mains, A. S. Quon, and B. A. Eipper. 1997. Peptidylglycine alpha-hydroxylating monooxygenase: active site residues, disulfide linkages, and a two-domain model of the catalytic core. Biochemistry. 36:10901-10909.
14. Blackburn, N. J., F. C. Rhames, M. Ralle, and S. Jaron. 2000. Major changes in copper coordination accompany reduction of peptidylglycine monooxygenase: implications for electron transfer and the catalytic mechanism. J. Biol. Inorg. Chem. 5:341-353.
15. Prigge, S. T., B. A. Eipper, R. E. Mains, and L. M. Amzel. 2004. Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. Science. 304:864-867.
16. Jaron, S., and N. J. Blackburn. 1999. Does Superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity. Biochemistry. 38:15086-15096.
17. The ccp4 suite: programs for protein crystallography. Collaborative computational project number 4. 1994. Acta Cryst. D50:760-763.
18. Navaza, J. 1994. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50:157-163.
19. Jones, T. A., Z.-Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119.
20. Murshudov, G. N., A. A. Vagin, and E. J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53:240-255.
21. Lamzin, V. S., and K. S. Wilson. 1997. Automated refinement for protein crystallography. Methods Enzymol. 277:269-305.
22. Lovell, S. C., I. W. Davis, W. B. Arendall III, P. I. W. de Bakker, J. M. Word, M. G. Prisant, J. S. Richardson, and D. C. Richardson. 2003. Structure validation by c-alpha geometry: phi, psi, and c-beta deviation. Proteins Struct. Funct. Genet. 50:437-450.
23. Jaron, S., and N. J. Blackburn. 2001. Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper. Biochemistry. 40:6867-6875.
24. Chen, P., J. Bell, B. A. Eipper, and E. I. Solomon. 2004. Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate. Biochemistry. 43:5735-5747.
25. Chen, P., and E. I. Solomon. 2004. Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site. J. Am. Chem. Soc. 126:4991-5000.
26. Vachette, P., E. Dainese, V. B. Vasyliev, P. Di Muro, M. Beltramini, D. I. Svergun, V. De Filippis, and B. Salvato. 2002. A key structural role for active site type 3 copper ions in human ceruloplasmin. J. Biol. Chem. 277:40823-40831.
27. Gatto, S., V. De Filippis, F. Spinozzi, P. Di Muro, L. Bubacco, and M. Beltramini. 2004. Structural role of the copper ions in the dinuclear active site of Carcinus aestuarii hemocyanin. Micron. 35:43-44.
28. Gray, H. B., B. G. Malmstrom, and R. J. Williams. 2000. Copper coordination in blue proteins. J. Biol. Inorg. Chem. 5:551-559.
29. Southan, C., and L. I. Kruse. 1989. Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain. FEBS Lett. 255:116-120.
30. Eipper, B. A., R. E. Mains, and C. C. Glembotski. 1983. Identification in pituitary tissue of a peptide alpha-amidation activity that acts on glycine-extended peptides and requires molecular oxygen, copper, and ascorbic acid. Proc. Natl. Acad. Sci. USA. 80:5144-5148.
31. Prigge, S. T., R. E. Mains, B. A. Eipper, and L. M. Amzel. 2000. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Cell. Mol. Life Sci. 57:1236-1259.
32. Brunger, A. T. 1992. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:472-475.
33. Kraulis, P. J. 1991. MolScript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
34. DeLano, W. L. 2002. The PyMOL Molecular Graphics System, http:// www.pymo1.org, W.L. DeLano Scientific, San Carlos, CA.