Myoglobin variants

Efficient conversion of primary azides to aldehydes catalyzed by active site variants of myoglobin.

The oxidation of primary azides to aldehydes constitutes a convenient but underdeveloped transformation for which no efficient methods are available. Here, we demonstrate that engineered variants of the hemoprotein myoglobin can catalyze this transformation with high efficiency (up to 8,500 turnovers) and selectivity across a range of structurally diverse aryl-substituted primary azides. Mutage...

Myoglobin expression: early induction and subsequent modulation of myoglobin and myoglobin mRNA during myogenesis.

We showed that myoglobin gene transcription and the appearance of myoglobin occur very early in myogenesis, in both humans and mice. In contrast to the contractile protein genes, there is a subsequent increase of 50- to 100-fold in myoglobin mRNA and protein levels during later muscle development. Myoglobin and myoglobin mRNA are present at elevated levels in fetal heart and are also detectable...

Case Study: Myoglobin

Myocardial myoglobin oxygen tension.

COBURN, R. F., F. PLOEGMAKERS, P. GONDRIE, AND R. ABBOUD. Myocardial myoglobin oxygen tension. Am. J. Physiol. 224(4): 870-876. 1973.-We have applied our method of estimating mean myoglobin oxygen tension from measurements of carbon monoxide binding to myoglobin to the in vivo canine myocardium. Carbon monoxide binding to myoglobin was determined with measurements of 14C0 in myocardial biopsy s...

Myoglobin function reassessed.

The heart and those striated muscles that contract for long periods, having available almost limitless oxygen, operate in sustained steady states of low sarcoplasmic oxygen pressure that resist change in response to changing muscle work or oxygen supply. Most of the oxygen pressure drop from the erythrocyte to the mitochondrion occurs across the capillary wall. Within the sarcoplasm, myoglobin,...