Influence of heme orientation on oxygen affinity in native sperm whale myoglobin

Livingston, David J.; Davis, Nicki L.; Mar, Gerd N. La; Brown, W. Duane

doi:10.1021/ja00322a043

Cited by 41 publications

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“…Spectra froin MbCN reveal more clearly that the heterogeneity originates froin heme disorder and is not due to a contiimination of the purified protein (Kreutzer, U. and Jue, T., unpublished results). It remains unclear whether the disordered heme also exerts a struclure/fhction interaction that modulates oxygen binding affinity or plays a significant role in regulating oxygen metabolism (Livingston et al, 1984;Light et al, 3987).…”

Section: Resultsmentioning

confidence: 99%

¹H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

Kreutzer¹,

Jue²

1996

European Journal of Biochemistry

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Key questions on how intertidal unimals adapt lo hypoxic stress center on the high energy phosphate response to decreasing oxygenation. With recent 'HP'P-NMR techniques to monitor inaniinalian tissue metabolism, ii novel approach has emerged to observe potentially the intracelliilar oxygen interaction in invertebrates. The present study indicates that Arenicoln marinn, a standard model for intertidal animals, exhibits ii distinct set of Mb 'H-NMR signals in vivo, corresponding to the two isolated Mb isoforms.Specitically both duoxy-Mb I and deoxy-Mb IT exhibit paramugnetically shifted signals at 93.4 ppm and 92.5 ppm at 25 "C, respectively, which arise from the proximal histidyl N,sH. Thesc signals retlcct the cellular oxygenation state and indicate clearly that the phasphotautocyainine levcl begins to drop at thc onset of anoxia and declines gradually to 50% of control after 3.5 h. 'H Mb spectra indicate protein heterogeneity originaling from heme as well as structural disorder.Keywords: NMR; oxygen; invertebrate; myoglobin; hypoxia.Many intertidal animals must cope with hypoxic stress and have adapted metabolic strategies to preserve their functional integrity by down-regulating thcir energy utilization and by compensating the aerobic energy loss with anaerobic ATP production (Hochachka and Guppy, 1987; Cirieshaber et a]., 1994). In particular the lugworm, Arenicolo mwincr has served as ii unique model to study the specific metabolic adaptations (Schiittler et al., 1983; Siegrnund ct al., 198s; Schiittler, 1986). From the work with A. rizorina and other hypoxia tolerant invertebrates researchers have established pivotal roles for glycogcnolysis and mitochondria) fermentation pathways leading to the formation of end products, such as opines, succinate and volatile fatty iicids (Bicudo, 1993; Grieshaber ct al., 1994).As with several invertebrates, A. mtrrii~o is an oxyconfortncr whose physiological charactcristios include it gradually clecreasing oxygen consumption in response la declining ambient oxygen tension. This decline in aerobic metabolism starts well above the critical oxygen point, which defines the transition to anaerobiosis (Tnulmond and Tchernigovtzcff, 1984 ; Piirtner und Grieshaber, 1993). In contrast oxyregulating organisins maintain a relatively constant oxygen consumption above the critical 0, point. Even though the A. nzuriizu oxygen-consuinption profile versus ambient 0, is well cherackrized, the underlying biochemical mechanism is not completely clear. How does the cell regulate its oxygen consumption in response L o decreasing oxygen'! How does the cell signal anacrobic ATP production'? Whril is the rolc of inyoglobin in oxygen supply to tnitcschondria? To answer these questions requires the tneasurement of intraccllular oxygen in sivo.Extant techniques, however, arc often imprecise and are too invasive for in vivo application. Observing metabolite concenlra-L'rrrrspr,/zric,nce to LJ. Kreutzer, Instittit fur Zoophysiologic, Heinrich-Heine-Univcrsitlt,

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Section: Resultsmentioning

confidence: 99%

¹H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

Kreutzer¹,

Jue²

1996

European Journal of Biochemistry

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“…Studies on the functional consequences of haem disorder have indicated that the disordered form has a higher affinity for 02 than has the form predominant in the native protein (Livingston et al, 1984). We have undertaken investigations of the ligand-binding kinetics of native and reconstituted myoglobins by fast reaction techiques.…”

Section: Resultsmentioning

confidence: 99%

Characterization of haem disorder by circular dichroism

Aojula¹,

Wilson²,

Drake³

1986

Biochemical Journal

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“…For example, the Bohr effect of Chironomous hemoglobin,12 the heme reduction potential of cytochrome b 5 13 and the affinity and degree of cooperativity in dioxygen binding by HbA14 have been reported to depend on heme orientation. In the specific case of myoglobin, though early work15 had indicated that the reversed form of deoxyMb has a 10-fold higher oxygen affinity than the native form, later reports conclusively showed that both the O 2 and CO affinities of the reversed form are essentially the same as those for the native form 16,17. While no significant differences in ligand affinities of the two forms are observed, Yamamoto et al showed that the exchange rate of the N ε H proton of the E7 distal histidine in the reversed form of sperm whale metMb-CN is larger by a factor of 3-5 as compared to the native, while the exchange rates of the proximal His F8 N ε H protons were essentially equal for the native and reversed forms and further documented only small differences in the rates of autoxidation of the oxy complex and azide affinity of the metMb derivative 9…”

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Resonance Raman Interrogation of the Consequences of Heme Rotational Disorder in Myoglobin and Its Ligated Derivatives

2008

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Resonance Raman spectroscopy is employed to characterize heme site structural changes arising from conformational heterogeneity in deoxyMb and ligated derivatives, i.e., the ferrous CO (MbCO) and ferric cyanide (MbCN) complexes. The spectra for the reversed forms of these derivatives have been extracted from the spectra of reconstituted samples. Dramatic changes in the low-frequency spectra are observed, where newly observed RR modes of the reversed forms are assigned using protohemes that are selectively deuterated at the four methyl groups or at the four methine carbons. Interestingly, while substantial changes in the disposition of the peripheral vinyl and propionate groups can be inferred from the dramatic spectral shifts, the bonds to the internal histidyl imidazole ligand and those of the Fe−CO and Fe−CN fragments are not significantly affected by the heme rotation, as judged by lack of significant shifts in the ν(Fe−NHis), ν(Fe−C), and ν(C−O) modes. In fact, the apparent lack of an effect on these key vibrational parameters of the Fe−NHis, Fe−CO, and Fe−CN fragments is entirely consistent with previously reported equilibrium and kinetic studies that document virtually identical functional properties for the native and reversed forms.

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Influence of heme orientation on oxygen affinity in native sperm whale myoglobin

Cited by 41 publications

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¹H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

¹H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

Characterization of haem disorder by circular dichroism

Resonance Raman Interrogation of the Consequences of Heme Rotational Disorder in Myoglobin and Its Ligated Derivatives

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Influence of heme orientation on oxygen affinity in native sperm whale myoglobin

Cited by 41 publications

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1H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

1H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

Characterization of haem disorder by circular dichroism

Resonance Raman Interrogation of the Consequences of Heme Rotational Disorder in Myoglobin and Its Ligated Derivatives

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¹H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation

¹H‐NMR Signal of Arenicola marina Myoglobin in vivo as an Index of Tissue Oxygenation