title: Life without myoglobin.
abstract: Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals [1]. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria [1-3]. This cytoplasmic hemoprotein was the first protein to be subjected to definitive structural analysis and has been a subject of long-standing and ongoing interest to biologists [1-3]. Recently, we utilized gene disruption technology to generate mice that are viable and fertile despite a complete absence of myoglobin [4]. This unexpected result led us to reexamine existing paradigms regarding the function of myoglobin in striated muscle.
authors.affiliation: Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75390-8573, USA. garry@ryburn.swmed.edu
authors.forename: D J
authors.initials: DJ
authors.lastname: Garry
authors.forename: A
authors.initials: A
authors.lastname: Meeson
authors.forename: Z
authors.initials: Z
authors.lastname: Yan
authors.forename: R S
authors.initials: RS
authors.lastname: Williams
mesh_terms: D000818:Animals; D001692:Biological Transport; D005786:Gene Expression Regulation; D051379:Mice; D018345:Mice, Knockout; D018482:Muscle, Skeletal / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D009211:Myoglobin / Q000172:deficiency* / Q000235:genetics / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism
chemical_list: D009211:Myoglobin; D010100:Oxygen