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Cited by 647Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsNitric Oxide and Endothelin Effects

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

Stone, James R., Marletta, Michael A.·1994·Biochemistry
DOI 10.1021/bi00184a036
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Abstract

Nitric oxide (.NO) is a recently discovered signaling agent which plays a role in many biological processes such as vasodilation and neuronal synaptic transmission. The only receptor characterized thus far for .NO is the soluble form of guanylate cyclase (sGC). .NO increases the Vmax of sGC by 100-200-fold, probably by interacting with a heme moiety on the enzyme. Although several procedures exist for purifying sGC, these procedures result in preparations with low heme contents. Using a novel procedure, the enzyme has been purified to homogeneity from bovine lung with a heme content of approximately 1 heme/heterodimer. The UV-visible spectrum of the enzyme contains a Soret peak centered at 431 nm and a single broad alpha/beta peak at 555 nm indicative of a 5-coordinate ferrous heme with histidine as the axial ligand. The heme moiety does not bind oxygen but will readily bind .NO to form a 5-coordinate complex or carbon monoxide (CO) to form a 6-coordinate complex. Oxidation of the heme with ferricyanide shifts the Soret to 393 nm, due most likely to the formation of a 5-coordinate ferric heme. In the ferric state, the heme will apparently not bind water but will bind cyanide with reduced affinity compared to methemoglobin and metmyoglobin. Purified enzyme containing 1 heme/heterodimer is activated 130-fold by .NO and 4.4-fold by CO.

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  • Excess superoxide or other ROS in the cell causes modification of different parts of the cellular machinery and is a known player in the genesis and progression of cardiovascular disease.

    “The excess of superoxide, or other ROS, in the cell causes the modification of different parts of the cellular machinery and is a known player in the genesis and progression of cardiovascular disease (227, 408, 409, 570, 672, 700, 893).”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [893]

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Authors
Stone, J. R., & Marletta, M. A.
Affiliations
University of Michigan (US)
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1994-05-10
Volume
33
Issue
18
Pages
5636-5640
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00184a036
OpenAlex
W2081347741
Cited by
647
References
30
Citations by year
2026: 4 · 2025: 10 · 2024: 7 · 2023: 11 · 2022: 12 · 2021: 13 · 2020: 11 · 2019: 13 · 2018: 13 · 2017: 23 · 2016: 12 · 2015: 15 · 2014: 19 · 2013: 23 · 2012: 30
FWCI
7.58
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • University of Michigan
  • National Institute of General Medical Sciences (T32-GM-07767, T32GM007767)
  • National Center for Research Resources (M-01RR00042, M01RR000042)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords
soluble guanylate cyclase, nitric oxide activation, carbon monoxide activation, heme, ferrous heme, ferric heme, heme coordination, UV-visible absorption spectrum, enzyme purification, bovine lung, cyanide binding, ferricyanide oxidation
MeSH terms
Animals, Carbon Monoxide, Cattle, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Ferric Compounds, Ferrous Compounds, Guanylate Cyclase, Heme, Lung, Nitric Oxide, Spectrophotometry, Ultraviolet

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