Chlorophyll-Komplexe mit Apo-Myoglobin und Albumin: Präparation, Stabilität und Photochemie
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- Type
- article
- Published
- 2005-12-19
- Cited by
- 3
- References
- 338
- Access
- Open access
- OpenAlex
- https://openalex.org/W1810776797
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:83469129
Keywords
Myoglobin, Chemistry, Biochemistry
References
- Structural factors governing hemin dissociation from metmyoglobin.
- Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering.
- Research advances in the use of tetrapyrrolic photosensitizers for photodynamic therapy.
- REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN.
- COMBINATION OF PROTOPORPHYRIN IX WITH SPERM WHALE APOMYOGLOBIN.
- Reconstitution of apomyoglobin with bile pigments
- THE GECMETRY AND ELECTRONIC STRUCTURE OF BIOLOGICALLY SIGNIFICANT MOLECULES AS OBSERVED BY NATURAL MAGNETIC OPTICAL ACTIVITY: I. PROTEIN CONFORMATION AND PLASTICITY, II. CHLOROPHYLL-CHLOROPHYLL INTERACTIONS, III. ELECTRONIC STRUCTURE OF METAL PORPHYRINS
- On the chemistry of pyrrole pigments, LXXXVII: The apomyoglobin heme pocket as a reaction vessel in bile pigment chemistry
- Linear dichroism of single crystals of the reaction center from Rhodobacter sphaeroides wild type strain 2.4.1
- Preparation of tetrapyrrole-amino acid covalent complexes
- Chemical Aspects of Photodynamic Therapy
- Photodynamic tumor therapy : quantitative data on 2nd and 3rd generation photosensitizers
- The Chemistry of Linear Oligopyrroles and Bile Pigments
- Biochemical Applications of Raman and Resonance Raman Spectroscopies
- Functional effects of heme orientational disorder in sperm whale myoglobin.
- CHANGES IN SIDE CHAIN REACTIVITY ACCOMPANYING THE BINDING OF HEME TO SPERM WHALE APOMYOGLOBIN.
- Structure of serum albumin.
- Porphyrins as photosensitizers.
- Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein.
- Interactions of bilirubin with bovine serum albumin in aqueous solution.
Cited by
- Myoglobin with chlorophyllous chromophores: influence on protein stability.
- Study of protein-bacteriochlorophyll and protein-lipid interactions of natural and model light-harvesting complex 2 in purple bacterium Rhodobacter sphaeroides.
- Inhibition of bacteriochlorophyll biosynthesis in the purple phototrophic bacteria Rhodospirillumrubrum and Rhodobacter capsulatus grown in the presence of a toxic concentration of selenite
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