نوع مقاله : مقاله پژوهشی

نویسندگان

1 دانشجوی ارشد . گروه زیست شناسی، واحد رودهن، دانشگاه آزاد اسلامی، رودهن، ایران

2 استادیار .گروه زیست شناسی، واحد رودهن، دانشگاه آزاد اسلامی، رودهن، ایران

10.22051/jab.2021.34174.1395

چکیده

در تحقیق حاضر موقعیت اسیدهای آمینه آروماتیک به عنوان عناصر مهم در تشکیل و پایداری ساختار سوم آنزیم پراکسیداز تربکوهی دناتوره شده با فلز روی، با کمک آنالیز گرافهای مشتق مرتبه دوم داده های طیف سنجی مورد بررسی قرار گرفته است. برای این منظور، مشتق مرتبه دوم گرافهای جذبی و نشری با 10 تکرار در محدوده ماوراء بنفش مرئی از طیف سنجی دورنگنمایی دورانی و فلورسانس برای آنزیم در حضور 500-100 میکرومولار کلرید روی با کمک نرم افزار متلب تهیه و مطالعه شده است. نتایج نشان می دهد که یون روی فشردگی میکروساختارهای اطراف اسیدهای آمینه آروماتیک را بویژه برای تریپتوفان کاهش داده است با اینحال حتی با غلظت 500 میکرو مولار روی، تریپتوفان مستقیما در معرض حلال آبدوست قرار نمی گیرد. بطورکلی به نظر می رسد که در واسرشتگی آنزیم توسط فلز روی، تریپتوفان اهمیت بیشتری نسبت به سایر اسیدهای آمینه آروماتیک دارد.

کلیدواژه‌ها

عنوان مقاله [English]

Evaluation of the aromatic amino acids microenvironments of zinc-denatured horseradish peroxidase; second- derivatives spectra analysis

نویسندگان [English]

  • Mohammad reza Rajabi 1
  • Najmeh Hadizadeh Shirazi 2

1 MSC Department of biology, Roudehen branch, Islamic Azad University, Roudehen, Iran

2 Assistant Professor, Department of biology, Roudehen branch, Islamic Azad University, Roudehen, Iran

چکیده [English]

In the present study, the position of aromatic amino acids as important elements in the formation and stability of the tertiary structure of zinc-denatured peroxidase has been investigated with the help of second-derivative graph analysis of spectroscopic data. For this purpose, the second- derivative of absorption and emission graphs with 10 replications in the visible UV range of circular dichroism and fluorescence spectroscopy for the enzyme in the presence of 500-100 μM zinc chloride was prepared and studied with the help of MATLAB software. The results show that zinc ions reduce the compaction of microstructures around aromatic amino acids, especially for tryptophan. However, even at a concentration of 500 μM zinc, tryptophan is not directly exposed to the hydrophilic solvent. In general, tryptophan seems to be more important than other aromatic amino acids in inhibiting the enzyme by zinc metal.

کلیدواژه‌ها [English]

  • Tryptophan
  • Tertiary structure
  • unfolding
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