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C K Chang

Publications and source records attributed to C K Chang.

At least 109 records · Page 6Linked to original sources
PubMed1987

Probing the structure and stability of the tumor-localizing derivative of hematoporphyrin by reductive cleavage with LiAlH4.

A procedure involving the use of the reducing agent lithium aluminum hydride (LiAlH4) has been designed to explore the nature of the oligomer linkages in the tumor-localizing component of hematoporphyrin derivative (HPD). High-performance liquid chromatography and fast-atom bombardment mass spectrometry were used to determine the reduction products. The results are consistent with a structure wherein ester linkages join hematoporphyrin molecules. The presence of minor amounts of ether-linked porphyrins was confirmed, and their origin was determined through the application of the chemical reduction process to HPD. An increased proportion of ether-linked porphyrins was detected during storage of HPD at room temperature or above. The commercial product Photofrin II, presumably an HPD preparation enriched in the dimer/oligomer fraction, was found to contain approximately 50% ether linkages. This product therefore differs from the corresponding fraction of freshly prepared HPD.

Aluminum↗
PubMed1987

Resonance Raman studies of sterically hindered cyanomet "strapped" hemes. Effects of ligand distortion and base tension on iron-carbon bond.

We report resonance Raman studies of the iron-carbon bond stretching vibrations, nu(Fe-CN), in sterically hindered and unhindered heme (FeIII)-CN- complexes. The sterically hindred "strapped hemes" are equipped with a covalently linked 13-, 14-, or 15-atom hydrocarbon chain across one face of the heme; these are called FeSP-13, FeSP-14, and FeSP-15, respectively. These straps would presumably exert a sideway shearing strain to force the linear ligands (e.g., CN- and CO) to be tilted and/or bent. The shorter the chain length, the weaker the ligand binding affinity because of a greater steric hindrance. This study reveals that the nu(Fe-CN) frequency decreases as the chain length is decreased, in contrast with the CO complexes, where the nu(Fe-CO) frequency increases as the chain length is decreased. For the heme-CN- complexes (with N-methylimidazole as a base), the nu(Fe-CN) frequencies are: heme 5 (unhindered), 451 cm-1; FeSP-15, 447 cm-1; FeSP-14, 447 cm-1; FeSP-13, 445 cm-1. For the heme-CO complexes (with N-methylimidazole as a base), the nu(Fe-CO) frequencies are: heme 5, 495 cm-1; FeSP-15, 509 cm-1; FeSP-14, 512 cm-1; FeSP-13, 514 cm-1 (Yu, N.-T., E. A. Kerr, B. Ward, and C. K. Chang, 1983, Biochemistry, 22:4534-4540). We have also studied the cyanide complexes with three different bases (pyridine, N-methylimidazole and 1,2-dimethylimidazole), and found that the trans-effect of cyanide complex is different from that of CO complexes. The tension on Fe"'-base bond weakens the Fe"'-CN- bond, whereas the tension on Fe"-base bond strengthens the Fe"-CO bond. The origin of these differences may be attributed to different extents of the d7r(Fe)- wr*(ligand) back bonding between the CN- and CO heme complexes. The Fe-C-N bending vibrations in these cyanomet strapped hemes are not resonance-enhanced, although this bending mode has been detected at -410 cm-' via Soret excitation in cyanometinsect hemoglobins. It is suggested that the orientation of the tilted Fe-C-N unit may be important in determining the overlap between CN and porphyrin 7r* orbitals, which provide coupling of the Fe-C-N bending mode with the resonant Soret (r-7r*) transition.

Heme↗
PubMed1987

Resonance Raman studies of dioxygen and carbon monoxide binding to imidazole-appended hemes.

Resonance Raman spectroscopy has been employed to probe the effects of proximal base strain on the bonding of O2 and CO in three synthetic hemins with covalently linked imidazole ligands. The strain is introduced by varying the length of the imidazole-containing side chain and by restricting the side chain flexibility with a phenyl ring. These hemins are abbreviated as "long," "short," and "stiff" hemins, respectively. In the deoxy state, the iron-imidazole stretching frequencies [nu(Fe--N epsilon)] for long, short, and stiff hemins are detected at 200, 207, and 204 cm-1, respectively. The strain induced in the iron-imidazole bond by the short hemin results in a higher nu(Fe--N epsilon) frequency, in contrast to the strain induced by sterically hindered 2-methylimidazole or 1,2-dimethylimidazole complexes in which the Fe--N epsilon bond is tilted and lengthened, but the imidazole ring remains perpendicular to the heme plane. However, in the short hemin, the plane of the imidazole ring may not be perpendicular to the plane of the porphyrin, altering the amount of pi-interaction (hence the strength of Fe--N epsilon bond) and the nature of normal mode containing Fe--N epsilon bond stretching. Upon CO binding, we have observed the nu(Fe--CO) stretching frequencies at 497 (long), 499 (short), and 496 cm-1 (stiff), somewhat lower than those reported by Mitchell et al. (Inorg. Chem., 1985, 24:967) for the chelated-heme X CO complexes (i.e., 501-506 cm-1). This is the first report of an iron-oxygen-associated vibration observed in solution for an unprotected heme. The oxy complexes were formed by introducing dioxygen to the deoxy complexes at -700C. The isotope-sensitive line was detected at 576 cm- (1602) in oxy stiff hemin, which was shifted to 545 cm-1 upon 1802 substitution. This is perhaps the largest isotope shift (31 cm-') observed to date, compared with the usual 22-24 cm-'.For the long and short hemins, the iron-oxygen-associated vibration was detected at 574 and 573 cm-', respectively.These values are very similar to those observed(N-methylimidazole) and myoglobin/hemoglobin.

Carbon Monoxide↗
PubMed1986

Evidence that heme d1 is a 1,3-porphyrindione.

Heme d1 is the noncovalently associated heme prosthetic group of the bacterial nitrite reductase known as cytochrome cd1. Additional evidence has been obtained in support of a dioxoisobacteriochlorin, or 1,3-porphyrindione, skeleton for this heme. The new data include the natural abundance 13C NMR spectrum of the free base methyl ester derivative of d1, mass spectrometric determinations of the molecular mass of the free base methyl ester and the Cu and the Zn chelates, visible and 1H NMR spectral comparisons between d1 and synthetic porphyrindione model compounds, and the isolation and characterization of several byproducts formed during the purification of the free base methyl ester of d1. The accumulated evidence strongly supports the following structure for the skeleton of d1: 1-oxo-2-methyl-2'-acetyl-3-oxo-4-methyl-4'-acetyl-5-methyl-6-acrylyl+ ++-7- propionyl-8-methylporphyrin.

Bacteria↗
PubMed1986

The porphinedione structure of heme d1. Synthesis and spectral properties of model compounds of the prosthetic group of dissimilatory nitrite reductase.

In an attempt to verify the recent proposal that the heme d1 prosthetic group isolated from cytochrome cd1 is not a chlorin, but a dioxo-isobacteriochlorin (Chang, C. K. (1985) J. Biol. Chem. 260, 9520-9522), a model dioxo-isobacteriochlorin has been synthesized possessing a pi-electron system exactly identical to that as proposed. The presence of an acrylic acid substituent strongly perturbs the absorption spectrum of the chromophore and produces a visible spectrum virtually indistinguishable from that of the iron-free heme d1. Based on this finding, buttressed by additional spectral correspondence between the model iron heme and heme d1, we conclude that the proposed diketo ring structure is indeed correct, and the trivial names "dioneheme" and "acryloporphyrindione" are suggested for heme d1 and the demetallated macrocycle, respectively.

Heme↗
PubMed1985

On the structure of heme d1. An isobacteriochlorin derivative as the prosthetic group of dissimilatory nitrite reductase?

Timkovich and co-workers have recently proposed a chlorin macrocycle structure for the heme d1 prosthetic group isolated from cytochrome cd1 of Pseudomonas aeruginosa and Paracoccus denitrificans (Timkovich, R., Cork, M. S., and Taylor, P. V. (1984) J. Biol. Chem. 259, 1577-1585; 15089-15093). However, this chlorin structure deduced by them is not entirely consistent with the spectral data. An alternative structure is proposed here based on the available spectral evidence. It is suggested that heme d1 in vivo is not a chlorin, but a dioxo-isobacteriochlorin having two adjacent pyrrole rings saturated.

Cytochrome c Group↗
PubMed1984

Kinetic study of CO and O2 binding to horse heart myoglobin reconstituted with synthetic hemes lacking methyl and vinyl side chains.

Carbon monoxide- and oxygen-binding rates and affinities were measured for horse heart myoglobins reconstituted with synthetic hemes lacking peripheral methyl and vinyl groups. There is an apparent correlation between heme size and ligand specificity, i.e. larger m values (ratios of CO vs O2 association rates, l'/k') with smaller hemes. However, this correlation broke down with the most dealkylated heme. This is interpreted as resulting from protein conformational changes altering the steric crowdedness at the O2-binding site. Spectral properties and autoxidation rates also corroborate this view.

Animals↗
PubMed1984

The toxic effects of triorganotin(IV) compounds on the culicine mosquito, Aedes aegypti (L).

The structure-activity relationships of 25 triorganotin(IV) compounds were studied using the 4th instar A. aegypti larvae of the susceptible Liverpool Red-eye strain. The LC50 values of these compounds were compared with those of Malathion, DDT and Temephos. Maximal activities were obtained with tritolyltin chloride and its complexes with triphenyl-phosphine oxide and pyridine N-oxide, dimethyloctyltin- and diethyloctyltin acetates and tributyltin sucrose phthalate. A limited number of the triorganotin compounds was also tested with observed high activity against the 4th instar larvae of a local DDT-tolerant strain and against the 2nd instar larvae and adults of the susceptible strain. Delayed effect studies with both 2nd and 4th instar larvae showed high post-treatment mortality for the latter and, among the range of active compounds, the methyl- and aryltin compounds, in particular, were also found to exhibit high residual activities (100% kill) in laboratory tests conducted up to 10 weeks.

Aedes↗
PubMed1984

Mean excitation energies for stopping powers in various materials composed of elements hydrogen through argon.

The basic model of Lindhard and Scharff, known as the local plasma model, is utilized to study the effects of the chemical and physical state of the medium on its stopping power. Unlike previous work with the local plasma model, in which individual electron shifts in the plasma frequency were estimated empirically, the Pines correction derived for a degenerate Fermi gas is shown herein to provide a reasonable estimate even on the atomic scale. Thus, the model is moved to a completely theoretical base requiring no empirical adjustments, adjustments characteristics of past applications. The principal remaining error is in the overestimation of the low-energy absorption properties characteristic of the plasma model in the region of the atomic discrete spectrum, although higher energy phenomena are accurately represented and even excitation-to-ionization ratios are given with fair accuracy. Mean excitation energies for covalently bonded gases and solids, ionic gases and crystals, and metals are calculated using first-order models of the bonded states for which reasonable agreement with the recently evaluated data of Seltzer and Berger is obtained. Hence the methods described herein allow reasonable estimates of mean excitation energy for any physical-chemical combination of material media for stopping power applications.

Aluminum↗
PubMed1983

Resonance Raman detection of Fe-CO stretching and Fe-C-O bending vibrations in sterically hindered carbonmonoxy "strapped hemes". A structural probe of Fe-C-O distortion.

We report resonance Raman studies of the Fe-C-O distortion in sterically hindered heme-CO complexes. The steric hindrance is provided by a hydrocarbon chain strapped across one face of the heme. Increasing the steric hindrance (by decreasing the chain length), which reduces the CO binding affinity, is found to increase the Fe-CO stretching frequencies: heme 5 (unstrapped), 495 cm-1; FeSP-15, 509 cm-1; FeSP-14, 512 cm-1; FeSP-13, 514 cm-1. This is interpreted in terms of a decrease in the CO effective mass and increased interactions between the C atom of CO and the N atom(s) of the pyrrole ring(s). Resonance Raman enhancement of the Fe-C-O bending mode upon Soret excitation may be correlated with the overlap between the porphyrin (pi*) and CO (pi*) orbitals when the CO ligand is tilted. Its intensity relative to that of the Fe-CO stretching mode increases with increasing steric hindrance in these "strapped hemes". In addition, we have estimated the Fe-C-O angles from isotope data in various heme-CO complexes. It is inferred that the angles are 167 +/- 5 degrees (FeSP-15) and 175 +/- 5 degrees (FeSP-14, FeSP-13, Mb X CO, and Hb X CO).

Carbon Monoxide↗
PubMed1983

Evaluation of the accuracy of the diff3/50 with a cell by cell comparison.

The traditional approach to the evaluation of accuracy of discrete differential counters uses a graphic comparison of automated and manual counts. This type of comparison introduces so much sampling variation that significant differences often are obscured. To exclude this sampling variability, one of three technologists, a reference technologist and the Coulter diff3/50, each performed a differential count on exactly the same 100 cells of 47 normal and 56 abnormal blood smears. Linear regression analysis demonstrated excellent agreement between the technologists for all cell types with the exception of band neutrophils. Comparison of the instrument results with the technologists' results showed very good agreement for segmented neutrophils, lymphocytes, monocytes, and eosinophils. The identification of band neutrophils, basophils, immature granulocytes and atypical lymphocytes requires improvement. The overall performance is acceptable, with only 11 leukocytes, on the average normal smear, misclassified out of 100 normal leukocytes (four bands called segs, four segs called bands, and three non-neutrophils incorrectly classified). We recommend similar evaluations for all discrete differential counters.

Basophils↗
PubMed1982

Picosecond photochemistry of a cofacial diporphyrin containing iron(III) and zinc(II): Mimicking electron transfer between cytochrome c and the primary electron donor in reaction centers of photosynthetic bacteria.

Comparison of picosecond kinetic and spectroscopic data for Zn octaethylporphine and Fe(III)Cl octaethylporphine with that for Zn-Fe(III)Cl, a cofacial diporphyrin composed of a Zn porphyrin covalently bound to an Fe(III)Cl porphyrin with two chains of five atoms each, supports the assignment of a light-driven electron transfer (k > 10(11)s(-1)) within Zn-Fe(III)Cl to form [Zn(+).-Fe(II)]Cl. The kinetics (k approximately 10(10)s(-1)) and thermodynamics of the reverse electron transfer are compared to those of a similar electron transfer in bacterial photosynthesis, the reduction of an oxidized bacteriochlorophyll dimer, (BChl)(2) (+)., by Fe(II) cytochrome c.

Journal Article↗
PubMed1981

Electron transport across glycerol monooleate bilayer lipid membranes facilitated by magnesium etiochlorin.

The transport of electrons across biological membranes is believed to play an important role in many biophenomena. Although there have been many examples of systems which may be transporting electrons across Mueller-Rudin bilayer lipid membranes (blm), none has been well characterized. The system we describe here comprises a glycerol monooleate blm containing a magnesium etiochlorin (Mg-C) separating two aqueous phases each containing ferricyanide, ferrocyanide, KCl, and a platinum electrode. The E0s for the Mg-C+/Mg-C and ferri-/ferrocyanide couples are 0.22 and 0.24 V vs. SCE. Thus the MG-C+/Mb-C system is easily poised by the ferri-/ferrocyanide system. When the potentials of the ferri-/ferrocyanide couples are different on each side of the blm we show that the open-circuit membrane potential nearly equals the difference between the redox potentials. This is unequivocal evidence that electrons are being transferred across the blm from one aqueous phase to the other. On the basis of these experiments we deduce that electron transport is the major charge transport mechanism. When redox potentials are the same on each side of the blm, the conductance of the membrane can be greater than 10(-3) S/cm2. The conductance is proportional to the second power of the concentration of Mg-C in the membrane-forming mixture. A number of additional experiments are described which attempt to elucidate the mechanism of electron transfer. We believe that our data are consistent with the idea of an electron-hopping mechanism in which the transmembrane electron transport occurs by a series of second-order electron transfers between membrane-bound electron donors (Mg-C) and acceptors (Mg-C+). Alternative explanations are presented.

Electron Transport↗