Journal ArticleDOI
Allosteric modulation by S-nitrosation in the low-O2 affinity myoglobin from rainbow trout
Signe Helbo,Angela Fago +1 more
TLDR
A novel, S-nitrosation-dependent allosteric mechanism in this low-affinity Mb that may contribute to targeted O₂-linked SNO release in the hypoxic fish heart and be of importance in preserving cardiac function during intense exercise is revealed.Abstract:
Myoglobin (Mb) serves in the facilitated diffusion and storage of O2 in heart and skeletal muscle, where it also regulates O2 consumption via nitric oxide (NO) scavenging or generation. S-nitrosati...read more
Citations
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Journal ArticleDOI
Hemoglobin βCys93 is essential for cardiovascular function and integrated response to hypoxia
Rongli Zhang,Douglas T. Hess,Zhaoxia Qian,Alfred Hausladen,Fabio V. Fonseca,Ruchi Chaube,James D. Reynolds,Jonathan S. Stamler +7 more
TL;DR: It is reported that mice with a βCys93Ala mutation are deficient in hypoxic vasodilation that governs blood flow autoregulation, the classic physiological mechanism that controls tissue oxygenation but whose molecular basis has been a longstanding mystery.
Journal ArticleDOI
Biomolecular Interactions Governing Fresh Meat Color in Post-mortem Skeletal Muscle: A Review.
TL;DR: This review examines how metabolites and mitochondrial activity can influence myoglobin oxygenation and metmyoglobin reducing activity and highlights recent research that has examined myoglobin redox dynamics, sarcoplasmic metabolite changes, and/or postmortem biochemistry.
Journal ArticleDOI
Hypoxia tolerance, nitric oxide, and nitrite: lessons from extreme animals.
Angela Fago,Frank B. Jensen +1 more
TL;DR: Recent work illustrating the widespread roles of NO and nitrite in the tolerance to extreme oxygen deprivation, in particular in the red-eared slider turtle and crucian carp, but also in diving marine mammals is highlighted.
Journal ArticleDOI
Insights into BAY 60-2770 Activation and S-Nitrosylation-Dependent Desensitization of Soluble Guanylyl Cyclase via Crystal Structures of Homologous Nostoc H-NOX Domain Complexes
Vijay Kumar,Faye Martin,Michael G. Hahn,Martina Schaefer,Jonathan S. Stamler,Johannes-Peter Stasch,Focco van den Akker +6 more
TL;DR: The structure reveals that BAY 60-2770 has displaced the heme and acts as a heme mimetic via carboxylate-mediated interactions with the conserved YxSxR motif as well as hydrophobic interactions, which could inhibit either heme incorporation or NO-activation of sGC and thus provide a structural basis for desensitization.
Journal ArticleDOI
Functional differentiation of myoglobin isoforms in hypoxia-tolerant carp indicates tissue-specific protective roles
Signe Helbo,Sylvia Dewilde,Daryl R. Williams,Herald Berghmans,Michael Berenbrink,Andrew R. Cossins,Angela Fago +6 more
TL;DR: Comparing the functional roles of these diverged myoglobin paralogs in the tolerance to severe hypoxia in the carp found Mb2 proved to be significantly faster at eliminating H(2)O(2,) a major in vivo reactive oxygen species (ROS), suggesting that this diverged Mb isoform may have a specific protective role against H( 2)O
References
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Book
Hemoglobin and myoglobin in their reactions with ligands
Eraldo Antonini,Maurizio Brunori +1 more
Journal ArticleDOI
Redox signaling: nitrosylation and related target interactions of nitric oxide.
Journal ArticleDOI
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
TL;DR: In this article, the role of S-nitrosohaemoglobin in the transduction of NO-related activities may have therapeutic applications, highlighting newly discovered allosteric and electronic properties of haemoglobin that appear to be involved in the control of blood pressure.
Book ChapterDOI
Linked functions and reciprocal effects in hemoglobin: a second look.
TL;DR: In this article, the authors discuss linked functions and reciprocal effects in hemoglobin and show that not only do the linkage relations apply irrespective of whether the macromolecules undergo chemical change or polymerization, but also whether the ligands themselves associate and dissociate, possibly as macromocules.
Journal ArticleDOI
Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient
Jonathan S. Stamler,Li Jia,Jerry P. Eu,Timothy J. McMahon,Ivan T. Demchenko,Joseph Bonaventura,Kim Gernert,Claude A. Piantadosi +7 more
TL;DR: By sensing the physiological oxygen gradient in tissues, hemoglobin exploits conformation-associated changes in the position of cysteinebeta93 SNO to bring local blood flow into line with oxygen requirements.
Related Papers (5)
Hypoxia tolerance in reptiles, amphibians, and fishes: life with variable oxygen availability.
Philip E. Bickler,Leslie T. Buck +1 more