Soluble Guanylate Cyclase from Bovine Lung: Activation with Nitric Oxide and Carbon Monoxide and Spectral Characterization of the Ferrous and Ferric States

Related Content

• Probing the Function of Heme Distortion in the H-NOX FamilyACS Chemical Biology

  • Probing the Function of Heme Distortion in the H-NOX Family

    Charles Olea, Jr., Elizabeth M. Boon, Patricia Pellicena, John Kuriyan and Michael A. Marletta
    ACS Chemical Biology 2008 3 (11), pp 703–710

    Abstract: Hemoproteins carry out diverse functions utilizing a wide range of chemical reactivity while employing the same heme prosthetic group. It is clear from high-resolution crystal structures and biochemical studies that protein-bound hemes are not planar and ...

    Abstract | Full Text HTML | PDF w/ Links | Hi-Res PDF
• Identification of Histidine 105 in the β1 Subunit of Soluble Guanylate Cyclase as the Heme Proximal LigandBiochemistry

  • Identification of Histidine 105 in the β1 Subunit of Soluble Guanylate Cyclase as the Heme Proximal Ligand

    Yunde Zhao, Johannes P. M. Schelvis, Gerald T. Babcock, and Michael A. Marletta
    Biochemistry 1998 37 (13), pp 4502–4509

    Abstract: Soluble guanylate cyclase isolated from bovine and rat lung is a heterodimeric hemoprotein composed of α1 and β1 subunits. The heme binding region has been localized to residues 1−385 of the β1 subunit [β1(1−385)], while the catalytic site(s) have been ...

    Abstract | Full Text HTML | Hi-Res PDF

Other ACS content by these authors:

• James R. Stone
• Michael A. Marletta