Picosecond and nanosecond geminate recombination of myoglobin with carbon monoxide, oxygen, nitric oxide and isocyanides

Jongeward, Karen A.; Magde, Douglas; Taube, Douglas J.; Marsters, James C.; Traylor, Teddy G.; Sharma, Vandna

doi:10.1021/ja00210a011

Cited by 151 publications

(144 citation statements)

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“…As a result, the observed ns time courses for geminate rebinding of O 2 show simple one or two exponential behavior at room temperature. These results contrast with the complex behavior observed for O 2 and CO rebinding at low temperatures (49,50) or for NO rebinding on picosecond time scales (9,23,24,30,51).…”

contrasting

confidence: 74%

“…However, the computed value of F geminate will be the same as that calculated from the side path parameters since both schemes can accurately represent the observed data, and F geminate is the experimentally defined total amplitude of geminate rebinding (17). In the linear scheme, kЈ entry represents the bimolecular rate of formation of state C, and the fitted rate parameters for the formation and decay of this secondary state will affect the overall association rate constant (29,30). In contrast, the rate parameters for the formation and decay of C state in the side path scheme have no influence on the steady state expressions for the overall association and dissociation rate constants.…”

Section: Methodsmentioning

confidence: 99%

“…Nitric oxide is the most reactive of the physiological gases, has the lowest quantum yield for complete photodissociation from the native myoglobin (Q Յ 0.01), and shows the largest amount of geminate recombination, F geminate Ն 0.99 (9,29,30). In effect, every time a NO molecule enters the distal pocket, it binds to the iron atom, and thus the rate-limiting step for the overall NO binding reaction is ligand entry.…”

Section: Methodsmentioning

confidence: 99%

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Mapping the Pathways for O2 Entry Into and Exit from Myoglobin

Scott

Gibson

Olson

2001

Journal of Biological Chemistry

356

585

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contrasting

confidence: 74%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Mapping the Pathways for O2 Entry Into and Exit from Myoglobin

Scott

Gibson

Olson

2001

Journal of Biological Chemistry

356

585

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“…The simulations were conducted with the Gromacs software (63). More details are provided in SI Materials and Methods (64)(65)(66)(67)(68)(69)(70)(71)(72)(73)(74).…”

Section: Methodsmentioning

confidence: 99%

Ultrafast anisotropic protein quake propagation after CO photodissociation in myoglobin

Brinkmann

Hub

2016

Proc. Natl. Acad. Sci. U.S.A.

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"Protein quake" denotes the dissipation of excess energy across a protein, in response to a local perturbation such as the breaking of a chemical bond or the absorption of a photon. Femtosecond timeresolved small-and wide-angle X-ray scattering (TR-SWAXS) is capable of tracking such ultrafast protein dynamics. However, because the structural interpretation of the experiments is complicated, a molecular picture of protein quakes has remained elusive. In addition, new questions arose from recent TR-SWAXS data that were interpreted as underdamped oscillations of an entire protein, thus challenging the long-standing concept of overdamped global protein dynamics. Based on molecular-dynamics simulations, we present a detailed molecular movie of the protein quake after carbon monoxide (CO) photodissociation in myoglobin. The simulations suggest that the protein quake is characterized by a single pressure peak that propagates anisotropically within 500 fs across the protein and further into the solvent. By computing TR-SWAXS patterns from the simulations, we could interpret features in the reciprocalspace SWAXS signals as specific real-space dynamics, such as CO displacement and pressure wave propagation. Remarkably, we found that the small-angle data primarily detect modulations of the solvent density but not oscillations of the bare protein, thereby reconciling recent TR-SWAXS experiments with the notion of overdamped global protein dynamics.time-resolved SAXS/WAXS | free-electron laser | molecular dynamics F unctional protein dynamics occur on various timescales, ranging from tens of femtoseconds for bond breaking, up to milliseconds and seconds for large-scale conformational transitions or protein folding. Observing and explaining such transitions, if possible in a time-resolved manner, has remained a central goal of molecular biophysics. A popular model system used to study proteins dynamics has been the 18-kDa protein myoglobin (Mb), the protein of first known tertiary structure (1). Mb contains an iron-porphyrin heme group that reversibly binds small gas molecules such as molecular oxygen (O 2 ) or carbon monoxide (CO). Mb is abundant in the muscle tissue of vertebrates, where it plays an important role in the transport and storage of O 2 and in the biochemistry of nitric oxide (2, 3).Because the CO-iron bonds in a Mb ensemble can be coherently photolysed with a laser flash within only 50 fs (4), a range of time-resolved techniques has been applied to probe various aspects of the structural dynamics after CO photodissociation, such as energy dissipation, CO dynamics, or heme doming (5-15). Three-dimensional movies of Mb conformational transitions were derived by means of time-resolved crystallography, which recently reached subpicosecond time resolution (16-19). These experimental studies were complemented by several pioneering molecular-dynamics (MD) simulations that revealed the Mb dynamics with atomic detail, with some focus on heat dissipation, vibrational dynamics, as well as ligand migration (20-28).Time-re...

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“…Redox cycling of myoglobin has been linked to oxidative myocardial damage observed during ischemia and reperfusion [9,10]. "NO reacts fairly rapidly with heme-proteins (k = 107 M-l.s -j) [11]. Nitrosylmyoglobin (MbNO) formation has been shown to mitigate the oxidate damage induced by myoglobin [12][13][14].…”

Section: Introductionmentioning

confidence: 99%

S‐Nitrosoglutathione induces formation of nitrosylmyoglobin in isolated hearts during cardioplegic ischemia — an electron spin resonance study

1996

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Previously, it has been shown that "NO donor S-nitrosoglutathione (GSNO) improves the postischemic functional recovery in crystalloid buffer-perfused isolated rat hearts subjected to cardioplegic ischemia. Supplementation of cardioplegic solution with nitronyl nitroxide, a scavenger of'NO, antagonized this protective effect. Using low temperature ESR, we have detected nitrosylmyoglobin (MbNO) in rat hearts subjected to cardioplegic ischemia in the presence of GSNO (20--200/zmol/I). During aerobic reperfusion MbNO signal intensity gradually decreased, but persisted for up to 30 min of aerobic reperfusion. We conclude that MbNO is an endogenous marker of "NO release in myocardial tissues. Implications of MbNO formation are discussed with respect to cardioprotection during ischemia-and reperfusion-induced myocardial injury.

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Picosecond and nanosecond geminate recombination of myoglobin with carbon monoxide, oxygen, nitric oxide and isocyanides

Cited by 151 publications

References 0 publications

Mapping the Pathways for O2 Entry Into and Exit from Myoglobin

Mapping the Pathways for O2 Entry Into and Exit from Myoglobin

Ultrafast anisotropic protein quake propagation after CO photodissociation in myoglobin

S‐Nitrosoglutathione induces formation of nitrosylmyoglobin in isolated hearts during cardioplegic ischemia — an electron spin resonance study

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