Hurley JK - Search Results

1

An electrochemical, kinetic, and spectroscopic characterization of [2Fe-2S] vegetative and heterocyst ferredoxins from Anabaena 7120 with mutations in the cluster binding loop.

Weber-Main AM, Hurley JK, Cheng H, Xia B, Chae YK, Markley JL, Martinez-Júlvez M, Gomez-Moreno C, Stankovich MT, Tollin G. Weber-Main AM, et al. Among authors: hurley jk. Arch Biochem Biophys. 1998 Jul 15;355(2):181-8. doi: 10.1006/abbi.1998.0743. Arch Biochem Biophys. 1998. PMID: 9675025

2

Further characterization by site-directed mutagenesis of the protein-protein interface in the ferredoxin/ferredoxin:NADP+ reductase system from Anabaena: requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer.

Hurley JK, Medina M, Gomez-Moreno C, Tollin G. Hurley JK, et al. Arch Biochem Biophys. 1994 Aug 1;312(2):480-6. doi: 10.1006/abbi.1994.1335. Arch Biochem Biophys. 1994. PMID: 8037461

3

Charge reversal mutations in a conserved acidic patch in Anabaena ferredoxin can attenuate or enhance electron transfer to ferredoxin:NADP+ reductase by altering protein/protein orientation within the intermediate complex.

Hurley JK, Schmeits JL, Genzor C, Gómez-Moreno C, Tollin G. Hurley JK, et al. Arch Biochem Biophys. 1996 Sep 1;333(1):243-50. doi: 10.1006/abbi.1996.0387. Arch Biochem Biophys. 1996. PMID: 8806777

4

Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants.

Hurley JK, Weber-Main AM, Stankovich MT, Benning MM, Thoden JB, Vanhooke JL, Holden HM, Chae YK, Xia B, Cheng H, Markley JL, Martinez-Júlvez M, Gómez-Moreno C, Schmeits JL, Tollin G. Hurley JK, et al. Biochemistry. 1997 Sep 16;36(37):11100-17. doi: 10.1021/bi9709001. Biochemistry. 1997. PMID: 9287153

5

Iron-sulfur cluster cysteine-to-serine mutants of Anabaena -2Fe-2S- ferredoxin exhibit unexpected redox properties and are competent in electron transfer to ferredoxin:NADP+ reductase.

Hurley JK, Weber-Main AM, Hodges AE, Stankovich MT, Benning MM, Holden HM, Cheng H, Xia B, Markley JL, Genzor C, Gomez-Moreno C, Hafezi R, Tollin G. Hurley JK, et al. Biochemistry. 1997 Dec 9;36(49):15109-17. doi: 10.1021/bi972001i. Biochemistry. 1997. PMID: 9398238

6

Role of hydrophobic interactions in the flavodoxin mediated electron transfer from photosystem I to ferredoxin-NADP+ reductase in Anabaena PCC 7119.

Nogués I, Martínez-Júlvez M, Navarro JA, Hervás M, Armenteros L, de la Rosa MA, Brodie TB, Hurley JK, Tollin G, Gómez-Moreno C, Medina M. Nogués I, et al. Among authors: hurley jk. Biochemistry. 2003 Feb 25;42(7):2036-45. doi: 10.1021/bi0270541. Biochemistry. 2003. PMID: 12590591

7

Mutations of surface residues in Anabaena vegetative and heterocyst ferredoxin that affect thermodynamic stability as determined by guanidine hydrochloride denaturation.

Hurley JK, Caffrey MS, Markley JL, Cheng H, Xia B, Chae YK, Holden HM, Tollin G. Hurley JK, et al. Protein Sci. 1995 Jan;4(1):58-64. doi: 10.1002/pro.5560040108. Protein Sci. 1995. PMID: 7773177 Free PMC article.

8

Structure-function studies of [2Fe-2S] ferredoxins.

Holden HM, Jacobson BL, Hurley JK, Tollin G, Oh BH, Skjeldal L, Chae YK, Cheng H, Xia B, Markley JL. Holden HM, et al. Among authors: hurley jk. J Bioenerg Biomembr. 1994 Feb;26(1):67-88. doi: 10.1007/BF00763220. J Bioenerg Biomembr. 1994. PMID: 8027024 Review.

9

Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis.

Hurley JK, Salamon Z, Meyer TE, Fitch JC, Cusanovich MA, Markley JL, Cheng H, Xia B, Chae YK, Medina M, et al. Hurley JK, et al. Biochemistry. 1993 Sep 14;32(36):9346-54. doi: 10.1021/bi00087a013. Biochemistry. 1993. PMID: 8369305

10

Structure-function relationships in the ferredoxin/ferredoxin: NADP+ reductase system from Anabaena.

Hurley JK, Fillat M, Gómez-Moreno C, Tollin G. Hurley JK, et al. Biochimie. 1995;77(7-8):539-48. doi: 10.1016/0300-9084(96)88170-3. Biochimie. 1995. PMID: 8589065

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