Abu-Soud HM - Search Results

1

Heme iron reduction and catalysis by a nitric oxide synthase heterodimer containing one reductase and two oxygenase domains.

Siddhanta U, Wu C, Abu-Soud HM, Zhang J, Ghosh DK, Stuehr DJ. Siddhanta U, et al. J Biol Chem. 1996 Mar 29;271(13):7309-12. doi: 10.1074/jbc.271.13.7309. J Biol Chem. 1996. PMID: 8631749 Free article.

2

High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin.

Wu C, Zhang J, Abu-Soud H, Ghosh DK, Stuehr DJ. Wu C, et al. Biochem Biophys Res Commun. 1996 May 15;222(2):439-44. doi: 10.1006/bbrc.1996.0763. Biochem Biophys Res Commun. 1996. PMID: 8670224

3

Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer.

Abu-Soud HM, Stuehr DJ. Abu-Soud HM, et al. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10769-72. doi: 10.1073/pnas.90.22.10769. Proc Natl Acad Sci U S A. 1993. PMID: 7504282 Free PMC article.

4

Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer.

Abu-Soud HM, Yoho LL, Stuehr DJ. Abu-Soud HM, et al. J Biol Chem. 1994 Dec 23;269(51):32047-50. J Biol Chem. 1994. PMID: 7528206 Free article.

5

Electron transfer in the nitric-oxide synthases. Characterization of L-arginine analogs that block heme iron reduction.

Abu-Soud HM, Feldman PL, Clark P, Stuehr DJ. Abu-Soud HM, et al. J Biol Chem. 1994 Dec 23;269(51):32318-26. J Biol Chem. 1994. PMID: 7528212 Free article.

6

Subunit dissociation and unfolding of macrophage NO synthase: relationship between enzyme structure, prosthetic group binding, and catalytic function.

Abu-Soud HM, Loftus M, Stuehr DJ. Abu-Soud HM, et al. Biochemistry. 1995 Sep 5;34(35):11167-75. doi: 10.1021/bi00035a023. Biochemistry. 1995. PMID: 7545434

7

Reconstitution of the second step in NO synthesis using the isolated oxygenase and reductase domains of macrophage NO synthase.

Ghosh DK, Abu-Soud HM, Stuehr DJ. Ghosh DK, et al. Biochemistry. 1995 Sep 12;34(36):11316-20. doi: 10.1021/bi00036a003. Biochemistry. 1995. PMID: 7547858

8

Neuronal nitric oxide synthase self-inactivates by forming a ferrous-nitrosyl complex during aerobic catalysis.

Abu-Soud HM, Wang J, Rousseau DL, Fukuto JM, Ignarro LJ, Stuehr DJ. Abu-Soud HM, et al. J Biol Chem. 1995 Sep 29;270(39):22997-3006. doi: 10.1074/jbc.270.39.22997. J Biol Chem. 1995. PMID: 7559438 Free article.

9

Control of electron transfer in neuronal nitric oxide synthase by calmodulin, substrate, substrate analogs, and nitric oxide.

Stuehr DJ, Abu-Soud HM, Rousseau DL, Feldman PL, Wang J. Stuehr DJ, et al. Adv Pharmacol. 1995;34:207-13. doi: 10.1016/s1054-3589(08)61087-x. Adv Pharmacol. 1995. PMID: 8562435 Review. No abstract available.

10

Domains of macrophage N(O) synthase have divergent roles in forming and stabilizing the active dimeric enzyme.

Ghosh DK, Abu-Soud HM, Stuehr DJ. Ghosh DK, et al. Biochemistry. 1996 Feb 6;35(5):1444-9. doi: 10.1021/bi9521295. Biochemistry. 1996. PMID: 8634274

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