Ultraviolet Raman spectroscopy indicates fast (less than 7 ns) R----T-like motion in hemoglobin.

Raman spectra of oxy- and deoxyhemoglobin obtained with 218 and 200 nm pulsed (7 ns) laser excitation show changes (loss of 880 cm-1 tryptophan band intensity, increase in the 830/850 cm-1 tyrosine doublet intensity ratio) which are attributed to the aromatic contacts (Trp beta 37-Tyr alpha 140 and Tyr alpha 42-Asp beta 99) that are specific to the T quaternary structure. At high concentration (2 mM in heme) HbCO shows the same spectral signatures as HbO2. As the HbCO concentration is decreased, however, the spectra approach those shown by deoxy-Hb.

Alternative carbon monoxide binding modes for horseradish peroxidase studied by resonance Raman spectroscopy.

Resonance Raman (RR) spectroscopy and infrared spectroscopy have been used to characterize the three vibrational modes, CO and FeC stretching and FeCO bending, for carbon monoxide bound to reduced horseradish peroxidase, with the aid of 13CO and C18O isotope shifts. At high pH, one species, I, is observed, with nu FeC = 490 cm-1 and nu CO = 1932 cm-1. The absence of a band attributable to delta FeCO suggests a linear FeCO unit normal to the heme plane.

Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states.

Resonance Raman (RR) spectra are reported for CO-bound cytochrome c peroxidase (CCP). At low pH, two forms are observed: form II, with nu Fe-C = 530 cm-1 and delta FeCO = 585 cm-1, and form I, with nu Fe-C = 495 cm-1 and no detectable delta FeCO. They appear to have coincident nu CO infrared bands, at 1922 cm-1.

Resonance Raman spectroscopic evidence that carp deoxyhemoglobin remains in a T-like quaternary structure at high pH: implications for cooperativity.

Resonance Raman spectroscopy shows the Fe-proximal imidazole stretching band to shift from 215 to 219 cm-1 between human deoxyhemoglobin (deoxy-Hb) and a Hb sample which is 75% oxygenated, demonstrating that the T-R quaternary structure switch can be monitored by resonance Raman spectroscopy in native Hb at equilibrium. For deoxy-Hb from carp, the band is at 215 cm-1 at pH 9 as well as pH 6, contrary to previous reports of an elevated frequency at high pH. The invariance of this frequency over a large affinity difference is in contrast to a recent report of continuously varying vFe-ImH frequencies for human mutant deoxy-Hb's.

Resonance Raman evidence for an exchangeable protein hydrogen associated with the heme a group of cytochrome oxidase.

When cytochrome-c oxidase is soaked in D2O, downshifts of the cytochrome a formyl C = O stretching mode are seen in the resonance Raman (RR) spectra (413.1 nm excitation) of both the resting and reduced forms. Other changes observed in the reduced protein RR spectra are consistent with involvement of the cytochrome a formyl group in the deuterium effect.

63/65Cu and 1/2H2O isotope shifts in the low-temperature resonance Raman spectrum of fungal laccase.

Resonance Raman spectra are reported for the type 1 Cu site of fungal laccase at 295 and 77 K. The low-temperature spectra show enhanced resolution and reveal several weak bands not previously observed, as well as overtone and combination bands associated with the strong approximately equal to 400 cm-1 fundamentals. A novel low-temperature Raman difference technique has been used to obtain 63/65Cu and 1/2H2O isotope shifts.

Pharmacokinetics of intravenous clindamycin in newborn infants.

We studied 12 newborn infants (gestational ages 26-39 wk [mean +/- SD, 30.6 +/- 4.7]; birth weight 640-2700 g, [mean, 1,322 +/- 688]; postnatal age 1-24 days [mean, 9.

Resonance Raman spectroscopy shows different temperature-dependent coordination equilibria for native horseradish and cytochrome c peroxidase.

Resonance Raman spectra are reported for native horseradish peroxidase (HRP) and cytochrome c peroxidase (CCP) at 290, 77 and 9 K, using 406.7 nm excitation, in resonance with the Soret electronic transition. The spectra reveal temperature-dependent equilibria involving changes in coordination or spin state.

Resonance Raman spectroscopy of pyridoxal Schiff bases.

Resonance Raman (RR) spectra are reported for amino acid and amine adducts of pyridoxal 5'-phosphate (PLP) and 5'-deoxypyridoxal (5'-dPL) in aqueous solution. For the valine adducts, a detailed study has been carried out on solutions at pH and pD 5, 9, and 13, values at which the pyridine and imine protons are successively ionized, and on the adducts formed from 15N-valine, alpha-deuterovaline, and N-methyl-PLP. Good quality spectra were obtained, despite the strong fluorescence of pyridoxal Schiff bases, by adding KI as a quencher, and by exciting the molecules on the blue side of their absorption bands: 406.

Resonance Raman spectra of the pyridoxal coenzyme in aspartate aminotransferase. Evidence for pyridine protonation and a novel photochemical H/D exchange at the imine carbon atom.

Resonance Raman (RR) spectra are reported for aspartate aminotransferase from pig heart cytosol, and for inhibitor complexes. They are interpreted with reference to the previously analyzed spectra of pyridoxal phosphate (PLP) Schiff base adducts. This comparison shows that, as expected, the pyridine N atom is protonated in the native enzyme at pH 5, and in the glutarate complexes at pH 8.

Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct.

An actively and passively mode-locked Nd:YAG laser, producing 30-ps pulses of 1-mJ energy at 532 nm, has been used to photolyze (carbonmonoxy)myoglobin (MbCO) and generate its resonance Raman spectrum, which was recorded with a vidicon multichannel analyzer. The photoproduct spectrum was obtained by subtraction of the MbCO spectrum, obtained at lower incident power levels. Comparison with the spectrum of deoxyMb, obtained with the same apparatus, revealed frequency downshifts of approximately 4 cm-1, for bands at 1604, 1554, and 1542 cm-1, which are identified with porphyrin skeletal modes v10, v19, and v11.

Ultraviolet resonance Raman spectra of cytochrome c conformational states.

Ultraviolet resonance Raman (UV RR) spectra are reported for ferricytochrome c from tuna and horse heart at pH 1.6, 7, 10, and 13, representing distinct conformational states of the protein (states II, III, IV, and V, respectively). The spectra were obtained with pulsed laser excitation at 200 and 218 nm, via H2 Raman shifting the fourth harmonic output of a pulsed YAG laser.

Nanosecond transient resonance Raman spectra of the FeII-CO and FeIII-NO photolysis products of horseradish peroxidase.

Resonance Raman spectra, obtained with 7 ns pulsed laser excitation, are reported for the photoproducts of the FeII-CO and FeIII-NO adducts of horseradish peroxidase. The porphyrin skeletal frequencies are the same as those observed for unligated FeII and FeIII (native) horseradish peroxidase, respectively. The absence of unrelaxed spectra is discussed in relation to the photoproduct frequency shifts and relaxations observed previously for hemoglobin.

Ultraviolet resonance Raman spectra of insulin and alpha-lactalbumin with 218- and 200-nm laser excitation.

Ultraviolet resonance Raman (RR) spectra, with 200- and 218-nm excitation from a H2-shifted quadrupled Nd:YAG laser, are reported for insulin and alpha-lactalbumin in dilute aqueous solution, at pH values known to produce differences in the exposure of the aromatic residues to solvent. At 200 nm, the spectra are dominated by tyrosine bands, whose intensity is lowered somewhat in protein conformations in which tyrosine is exposed to solvent. The expected shift in the relative intensities of the components of the approximately 850-cm-1 tyrosine doublet is difficult to discern because the higher energy component shows much greater resonance enhancement and the lower energy component appears as a weak shoulder.

Resonance Raman spectroscopy and enhanced photoreducibility for the 420 nm pulsed form of cytochrome oxidase.

Resonance Raman (RR) spectra, with 413.1 nm Kr+ laser excitation, are reported for cytochrome oxidase in resting, reduced, and 428 nm (oxygenated) forms, and for the first time, in the 420 nm (pulsed) forms [(1984) J. Biol.

Oral neomycin sulfate and erythromycin base before colon surgery: a comparison of serum and tissue concentrations.

It is accepted that the use of oral neomycin sulfate and erythromycin base before colon surgery results in decreased numbers of intestinal bacteria. Intraluminal levels of these agents are reported to be very high, but systemic availability is still debated. The systemic levels were studied in 8 patients undergoing colon surgery.

Resonance Raman spectroscopy as a probe of heme protein structure and dynamics.

Our understanding of metalloporphyrin resonance Raman spectra has advanced to the point where it is possible to obtain detailed information about the structure of the heme group in situ in heme proteins. The porphyrin skeletal mode frequencies can be analyzed in terms of the ligation and spin state of the heme and may provide information about protein-induced stresses. The high-frequency region of the spectrum also contains bands due to vibrations of the porphyrin peripheral substituents, which are potentially monitors of the protein contacts.

[Differential diagnosis of primary bone tumors and tumor-like lesions of the ribs].

Primary bone tumours in ribs are less common than tumour-like lesions. The most common solitary primary bone tumour in ribs is the chondrosarcoma (about 35%). This is followed with about the same frequency (10 to 14%) by Ewing's sarcoma, malignant lymphoma, chondroma and osteo-chondromas.

Thymopoietin pentapeptide (thymopentin, TP-5) in the treatment of rheumatoid arthritis. A compilation of several short- and longterm clinical studies.

Thymopentin (TP-5), the active side of thymopoietin, was shown to affect immunoregulation. The effect of this drug in the treatment of rheumatoid arthritis (RA) was evaluated. Three trials were performed: a six month double-blind trial comparing TP-5 administered subcutaneously to placebo at 3 different dosages, an open longterm study in which the same dosage of the drug was administered subcutaneously, and a shortterm (3 weeks) double-blind trial in which the drug was given intravenously at a high dosage (100 mg/day).

Extended X-ray absorption fine structure study of the coupled binuclear copper active site of tyrosinase from Neurospora crassa.

Cu K-edge X-ray absorption spectra have been recorded for the enzyme tyrosinase from Neurospora crassa, in its oxy, resting (met-aquo), and inhibitor-bound (met-mimosine) forms. The K-edges proper resemble those of oxy- and met-hemocyanin, and confirm the presence of CuII. The forbidden 1s----3d transition is noticeably stronger for the 1-mimosine-bound enzyme, implying some distortion of the tetragonal Cu coordination group on inhibitor binding.

X-ray absorption study of Rhus laccase: evidence for a copper-copper interaction, which disappears on type 2 copper removal.

X-ray absorption spectra are reported for the multi-Cu oxidase Rhus vernicifera laccase in oxidized and fully reduced forms and for laccase from which the type 2 Cu has been depleted (T2D). The structure of the Cu K edge for both preparations shows the presence of CuII and CuI in the oxidized and reduced states, respectively. As previously reported by LuBien et al.

Resonance Raman studies of beef heart aconitase and a bacterial hydrogenase.

The resonance Raman (RR) spectra of beef heart aconitase and of an air-stable hydrogenase from Desulfuvibrio desulfuricans, as isolated, are characteristic of 3Fe centers. Activation of aconitase by Fe(II) addition converts the RR spectrum to one characteristic of [4Fe-4S]2+ clusters. Analytical data on aconitase, as isolated, confirms the recent finding (Beinert, H.

Resonance Raman spectra of flavin semiquinones stabilized by N5 methylation.

Resonance Raman spectra are reported for the semiquinone of N5-methyl derivatives of FMN (flavin mononucleotide) in H2O and 2H2O, 8-chloro FMN and FAD (flavin adenine dinucleotide) with 647.1 nm excitation, in the first pi-pi absorption band, using KI to quench fluorescence. The spectral pattern is similar to that of oxidized flavin, in its first absorption band, but with appreciable shifts, up to approx.