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Items: 1 to 20 of 244

1.

Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids.

Berry SM, Ralle M, Low DW, Blackburn NJ, Lu Y.

J Am Chem Soc. 2003 Jul 23;125(29):8760-8.

PMID:
12862470
2.

Reduction potential tuning of the blue copper center in Pseudomonas aeruginosa azurin by the axial methionine as probed by unnatural amino acids.

Garner DK, Vaughan MD, Hwang HJ, Savelieff MG, Berry SM, Honek JF, Lu Y.

J Am Chem Soc. 2006 Dec 13;128(49):15608-17.

PMID:
17147368
3.

Axial methionine has much less influence on reduction potentials in a CuA center than in a blue copper center.

Hwang HJ, Berry SM, Nilges MJ, Lu Y.

J Am Chem Soc. 2005 May 25;127(20):7274-5.

PMID:
15898751
4.

X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin.

Romero A, Hoitink CW, Nar H, Huber R, Messerschmidt A, Canters GW.

J Mol Biol. 1993 Feb 20;229(4):1007-21.

PMID:
8383207
5.
6.

Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin.

Hall JF, Kanbi LD, Strange RW, Hasnain SS.

Biochemistry. 1999 Sep 28;38(39):12675-80.

PMID:
10504237
7.

Structural characterization of azurin from Pseudomonas aeruginosa and some of its methionine-121 mutants.

Murphy LM, Strange RW, Karlsson BG, Lundberg LG, Pascher T, Reinhammar B, Hasnain SS.

Biochemistry. 1993 Mar 2;32(8):1965-75.

PMID:
8383530
8.

The selenocysteine-substituted blue copper center: spectroscopic investigations of Cys112SeCys Pseudomonas aeruginosa azurin.

Ralle M, Berry SM, Nilges MJ, Gieselman MD, van der Donk WA, Lu Y, Blackburn NJ.

J Am Chem Soc. 2004 Jun 16;126(23):7244-56.

PMID:
15186162
9.

Transforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation.

Clark KM, Yu Y, Marshall NM, Sieracki NA, Nilges MJ, Blackburn NJ, van der Donk WA, Lu Y.

J Am Chem Soc. 2010 Jul 28;132(29):10093-101. doi: 10.1021/ja102632p.

10.
11.

Effect of pH and ligand binding on the structure of the Cu site of the Met121Glu mutant of azurin from Pseudomonas aeruginosa.

Strange RW, Murphy LM, Karlsson BG, Reinhammar B, Hasnain SS.

Biochemistry. 1996 Dec 17;35(50):16391-8.

PMID:
8973215
12.

A selenomethionine-containing azurin from an auxotroph of Pseudomonas aeruginosa.

Frank P, Licht A, Tullius TD, Hodgson KO, Pecht I.

J Biol Chem. 1985 May 10;260(9):5518-25.

13.

Cassette mutagenesis of Met121 in azurin from Pseudomonas aeruginosa.

Karlsson BG, Nordling M, Pascher T, Tsai LC, Sjölin L, Lundberg LG.

Protein Eng. 1991 Feb;4(3):343-9.

PMID:
1649999
14.

The role of hydrogen bonding at the active site of a cupredoxin: the Phe114Pro azurin variant.

Yanagisawa S, Banfield MJ, Dennison C.

Biochemistry. 2006 Jul 25;45(29):8812-22.

PMID:
16846224
15.

X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu.

Karlsson BG, Tsai LC, Nar H, Sanders-Loehr J, Bonander N, Langer V, Sjölin L.

Biochemistry. 1997 Apr 8;36(14):4089-95.

PMID:
9100002
16.

The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin.

Jeuken LJ, Ubbink M, Bitter JH, van Vliet P, Meyer-Klaucke W, Canters GW.

J Mol Biol. 2000 Jun 9;299(3):737-55.

PMID:
10835281
17.
18.

Loop-contraction mutagenesis of type 1 copper sites.

Yanagisawa S, Dennison C.

J Am Chem Soc. 2004 Dec 8;126(48):15711-9.

PMID:
15571393
19.

Effect of lysine ionization on the structure and electrochemical behaviour of the Met44-->Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa.

Van de Kamp M, Canters GW, Andrew CR, Sanders-Loehr J, Bender CJ, Peisach J.

Eur J Biochem. 1993 Nov 15;218(1):229-38.

20.

Resonance Raman spectroscopy of the azurin His117Gly mutant. Interconversion of type 1 and type 2 copper sites through exogenous ligands.

den Blaauwen T, Hoitink CW, Canters GW, Han J, Loehr TM, Sanders-Loehr J.

Biochemistry. 1993 Nov 23;32(46):12455-64.

PMID:
8241136
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