Various Metallopheophorbides as Substrates for Chlorophyll Synthetase

نویسندگان

  • Michael Helfrich
  • Wolfhart Rüdiger
چکیده

Pheophorbide a was prepared from a mixture o f chlorophylls a and b by differential extrac­ tion with HC1 and saponification. The insertion o f the following metal ions was investigated: Mg, Zn, Co, Cu, Ni. In the enzyme test with chlorophyll synthetase, the metallopheophorbides fall into two categories: the Mgand Zn-complexes are good substrates, the Co-, Cuand Ni-complexes are neither substrates nor competitive inhibitors for the enzyme reaction. This corresponds to two categories o f complex structures: Mgand Zn-porphyrins prefer pentacoordinate square-pyramidal structures, Co-, Cuand Ni-porphyrins prefer tetracoordinate square-planar structures. A model for substrate binding to chlorophyll synthetase is proposed.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Chlorophyll Biosynthesis: Various Chlorophyllides as Exogenous Substrates for Chlorophyll Synthetase

The esterification of various chlorophyllides with geranylgeranyl diphosphate was investigated as catalyzed by the enzyme chlorophyll synthetase. The enzyme source was an etioplast membrane fraction from etiolated oat seedlings (Avena sativa L.). The following chlorophyllides were prepared from the corresponding chlorophylls by the chlorophyllase reaction: chlorophyllide a (2) and b (4), bacter...

متن کامل

Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Study of the interactions with its substrates.

The binding of the various substrates to Escherichia coli glutamyl-tRNA synthetase has been investigated by using as experimental approaches the binding study under equilibrium conditions and the substrate-induced protection of the enzyme against its thermal inactivation. The results show that ATP and tRNAGlu bind to the free enzyme, whereas glutamate binds only to an enzyme form to which gluta...

متن کامل

Aminoacyl-SNACs as small-molecule substrates for the condensation domains of nonribosomal peptide synthetases.

BACKGROUND Nonribosomal peptide synthetases (NRPSs) are large multidomain proteins that catalyze the formation of a wide range of biologically active natural products. These megasynthetases contain condensation (C) domains that catalyze peptide bond formation and chain elongation. The natural substrates for C domains are biosynthetic intermediates that are covalently tethered to thiolation (T) ...

متن کامل

A high-throughput screen for directed evolution of aminocoumarin amide synthetases.

The biosynthesis of aminocoumarin antibiotics involves the action of amide synthetases which construct amide bonds between aminocoumarins and various acyl moieties. Libraries of aminocoumarin analogues have been generated by in vivo fermentation, via feeding known amide synthetase substrates into producing microbial strains. Critically, such feeding studies rely on the inherent or engineered su...

متن کامل

One divinyl reductase reduces the 8-vinyl groups in various intermediates of chlorophyll biosynthesis in a given higher plant species, but the isozyme differs between species.

Divinyl reductase (DVR) converts 8-vinyl groups on various chlorophyll intermediates to ethyl groups, which is indispensable for chlorophyll biosynthesis. To date, five DVR activities have been detected, but adequate evidence of enzymatic assays using purified or recombinant DVR proteins has not been demonstrated, and it is unclear whether one or multiple enzymes catalyze these activities. In t...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013